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Conserved domains on  [gi|110815813|ref|NP_057460|]
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rabankyrin-5 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BTB_POZ_Rank-5 cd18303
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
50-169 5.05e-66

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1) or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms. It contains an N-terminal BTB domain, followed by a BACK domain, several ankyrin (ANK) repeats and a C-terminal FYVE domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


:

Pssm-ID: 349612 [Multi-domain]  Cd Length: 120  Bit Score: 217.96  E-value: 5.05e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   50 FISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFR 129
Cdd:cd18303     1 FISRLLKTVASLFDKELYSDITIKLADKSIPAHKFVLAARSEKWSNENLASTNELDLSDISYEVVLALLRWLYTDELDLT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 110815813  130 EDDVFLTELMKLANRFQLQLLRERCEKGVMSLVNVRNCIR 169
Cdd:cd18303    81 LDDEFLLELMKAAKRFQLTDLVERCERALMSSVNVDNCIR 120
BACK_ANKFY1_Rank5 cd18501
BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ...
162-250 1.02e-53

BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1), or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms.


:

Pssm-ID: 350576  Cd Length: 89  Bit Score: 181.68  E-value: 1.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  162 VNVRNCIRFYQTAEELNASTLMNYCAEIIASHWDDLRKEDFSSMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEM 241
Cdd:cd18501     1 VNVRNCIRFYQTAEEIGASTLREYCSEIISTHWDDLTPEDFAKMSAPLLYRMFKSKTKHPLHAAIRLKREDVVFLYLIEF 80

                  ....*....
gi 110815813  242 DSQLPGKLN 250
Cdd:cd18501    81 DSQLPGKLN 89
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
1102-1164 1.23e-46

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


:

Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 160.67  E-value: 1.23e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815813 1102 EPPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1164
Cdd:cd15728     1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
639-977 3.27e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 3.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  639 LFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcw 718
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  719 gpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVN 798
Cdd:COG0666    82 --AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR------------DKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  799 AQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHV 878
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETP----------------------------------LHL 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  879 AVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSV 958
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVN--AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 110815813  959 LLENGVDFAAVDENGNNAL 977
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
434-705 4.67e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 4.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  434 FDENSFAARLIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQ 513
Cdd:COG0666    30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  514 GANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVL 593
Cdd:COG0666   110 GADVNARDKDG-------------------ETPLHLAAYNGNLEIVKLLLEAGA-------------DVNAQDNDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  594 GLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAIRNQLPLVVD 673
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVK 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 110815813  674 AICTRGADMSVPDEKGNPPLWLALANNLEDIA 705
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
204-555 2.89e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 2.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  204 SMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEMDSQLPGKLNEADHNGDLALDLALSRRLESIATTLVSHKADVD 283
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  284 MVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNaATLGAQETPLHLVALYSSKKhsadvmsemaqIAEALLQAGANPNMQ 363
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLE-----------IVKLLLEAGADVNAQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  364 DSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLELKDHEGSTALWLAVQHitvssdqsvnpfEDVPVVNgtsfdensfaarl 443
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAEN------------GHLEIVK------------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  444 iqrgshtdapdtatgncllqraagagneaaalFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEE 523
Cdd:COG0666   204 --------------------------------LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
                         330       340       350
                  ....*....|....*....|....*....|..
gi 110815813  524 ALPLPKEAASLTSLADSVHLQTPLHMAIAYNH 555
Cdd:COG0666   252 GLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
Ank_2 pfam12796
Ankyrin repeats (3 copies);
944-1023 7.56e-11

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 7.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   944 LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAeafNLRGQSPLHILGQYGKENAA 1023
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
 
Name Accession Description Interval E-value
BTB_POZ_Rank-5 cd18303
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
50-169 5.05e-66

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1) or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms. It contains an N-terminal BTB domain, followed by a BACK domain, several ankyrin (ANK) repeats and a C-terminal FYVE domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349612 [Multi-domain]  Cd Length: 120  Bit Score: 217.96  E-value: 5.05e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   50 FISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFR 129
Cdd:cd18303     1 FISRLLKTVASLFDKELYSDITIKLADKSIPAHKFVLAARSEKWSNENLASTNELDLSDISYEVVLALLRWLYTDELDLT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 110815813  130 EDDVFLTELMKLANRFQLQLLRERCEKGVMSLVNVRNCIR 169
Cdd:cd18303    81 LDDEFLLELMKAAKRFQLTDLVERCERALMSSVNVDNCIR 120
BACK_ANKFY1_Rank5 cd18501
BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ...
162-250 1.02e-53

BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1), or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms.


Pssm-ID: 350576  Cd Length: 89  Bit Score: 181.68  E-value: 1.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  162 VNVRNCIRFYQTAEELNASTLMNYCAEIIASHWDDLRKEDFSSMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEM 241
Cdd:cd18501     1 VNVRNCIRFYQTAEEIGASTLREYCSEIISTHWDDLTPEDFAKMSAPLLYRMFKSKTKHPLHAAIRLKREDVVFLYLIEF 80

                  ....*....
gi 110815813  242 DSQLPGKLN 250
Cdd:cd18501    81 DSQLPGKLN 89
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
1102-1164 1.23e-46

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 160.67  E-value: 1.23e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815813 1102 EPPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1164
Cdd:cd15728     1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
639-977 3.27e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 3.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  639 LFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcw 718
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  719 gpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVN 798
Cdd:COG0666    82 --AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR------------DKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  799 AQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHV 878
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETP----------------------------------LHL 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  879 AVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSV 958
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVN--AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 110815813  959 LLENGVDFAAVDENGNNAL 977
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
434-705 4.67e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 4.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  434 FDENSFAARLIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQ 513
Cdd:COG0666    30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  514 GANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVL 593
Cdd:COG0666   110 GADVNARDKDG-------------------ETPLHLAAYNGNLEIVKLLLEAGA-------------DVNAQDNDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  594 GLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAIRNQLPLVVD 673
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVK 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 110815813  674 AICTRGADMSVPDEKGNPPLWLALANNLEDIA 705
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
1103-1164 2.10e-25

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 100.20  E-value: 2.10e-25
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813   1103 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1164
Cdd:smart00064    2 PHWIPDEEvsnCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDCYENL 66
PHA03095 PHA03095
ankyrin-like protein; Provisional
698-994 1.62e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 105.49  E-value: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  698 ANNLEDIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNEpTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHL 777
Cdd:PHA03095   23 SNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD-IVRLLLEAGADVNAP------------ERCGFTPLHL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  778 AASWGLEETV-QCLLEFGANVNAQDAEGRTPIHVAISSQ--HGVIIQLLVSHpDIHLNVRDRQGLTPFACAMtfKNNKSA 854
Cdd:PHA03095   90 YLYNATTLDViKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRK-GADVNALDLYGMTPLAVLL--KSRNAN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  855 EAILKR--ESGAAE-QVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAVQAGS--EIIVRNLLLA 929
Cdd:PHA03095  167 VELLRLliDAGADVyAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIA 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813  930 GAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHgrlNNIRVLLT 994
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN---NNGRAVRA 308
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
1103-1165 4.64e-23

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 93.60  E-value: 4.64e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813  1103 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPII-KFDLNKPVRVCNICFDVLT 1165
Cdd:pfam01363    1 PVWVPDSSatvCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpELGSNKPVRVCDACYDTLQ 67
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
204-555 2.89e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 2.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  204 SMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEMDSQLPGKLNEADHNGDLALDLALSRRLESIATTLVSHKADVD 283
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  284 MVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNaATLGAQETPLHLVALYSSKKhsadvmsemaqIAEALLQAGANPNMQ 363
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLE-----------IVKLLLEAGADVNAQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  364 DSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLELKDHEGSTALWLAVQHitvssdqsvnpfEDVPVVNgtsfdensfaarl 443
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAEN------------GHLEIVK------------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  444 iqrgshtdapdtatgncllqraagagneaaalFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEE 523
Cdd:COG0666   204 --------------------------------LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
                         330       340       350
                  ....*....|....*....|....*....|..
gi 110815813  524 ALPLPKEAASLTSLADSVHLQTPLHMAIAYNH 555
Cdd:COG0666   252 GLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
69-156 1.11e-16

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 76.58  E-value: 1.11e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813     69 DLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELD-----LSDANPEVTMTMLRWIYTDELEFREDDVFltELMKLAN 143
Cdd:smart00225    1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDkseiyLDDVSPEDFRALLNFLYTGKLDLPEENVE--ELLELAD 78
                            90
                    ....*....|...
gi 110815813    144 RFQLQLLRERCEK 156
Cdd:smart00225   79 YLQIPGLVELCEE 91
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
60-156 2.42e-16

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 75.76  E-value: 2.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813    60 DLYEQEQYSDLKIKVGDRHISAHKFVLAARSDS-WSLANL----SSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 134
Cdd:pfam00651    3 ELREQGELCDVTLVVGDKEFRAHKAVLAACSPYfKALFSGqeseSSVSEITLDDVSPEDFEALLEFMYTGKLISEENVD- 81
                           90       100
                   ....*....|....*....|..
gi 110815813   135 ltELMKLANRFQLQLLRERCEK 156
Cdd:pfam00651   82 --DLLAAADKLQIPSLVDKCEE 101
Ank_2 pfam12796
Ankyrin repeats (3 copies);
876-970 9.02e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 9.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   876 LHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRnLLLAGAKVNELTKHRqTALHLAAQQDLPTI 955
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDNGR-TALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 110815813   956 CSVLLENGVDFAAVD 970
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
307-580 1.75e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  307 FLIKNGAFVNAATL-GAqeTPLHLVALYSSKkhsADVMsemaqiaEALLQAGANPNMQDSKGRTPLHV--SIMAGNEYVF 383
Cdd:PHA03095   68 LLLEAGADVNAPERcGF--TPLHLYLYNATT---LDVI-------KLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  384 SQLLQcKQLDLELKDHEGSTALwlavqHITVSS------------DQSVNPFeDVPVVNGTSFDE--NSFAAR------L 443
Cdd:PHA03095  136 RLLLR-KGADVNALDLYGMTPL-----AVLLKSrnanvellrlliDAGADVY-AVDDRFRSLLHHhlQSFKPRarivreL 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  444 IQRGSHTDAPDtATGNCLLQRAAGAGNEAAAL---FLAtNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQ 520
Cdd:PHA03095  209 IRAGCDPAATD-MLGNTPLHSMATGSSCKRSLvlpLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813  521 TEEALplpkeaasltsladsvhlqTPLHMAIAYNHPDVVSVILEQK------ANAL-HATNNLQIIP 580
Cdd:PHA03095  287 SSDGN-------------------TPLSLMVRNNNGRAVRAALAKNpsaetvAATLnTASVAGGDIP 334
Ank_2 pfam12796
Ankyrin repeats (3 copies);
944-1023 7.56e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 7.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   944 LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAeafNLRGQSPLHILGQYGKENAA 1023
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
727-845 1.12e-10

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: 65.80  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  727 QTLLHRAIDENNEPTACFLIRSGCDVNSPRqpgANGEGEEEARD-----GQTPLHLAASWGLEETVQCLLEFGANVNAQD 801
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVSPR---ATGTFFRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 110815813  802 AEGRTPIHVAISSQHGV----IIQLLVSHpDIHLN------VRDRQGLTPFACA 845
Cdd:cd22192   167 SLGNTVLHILVLQPNKTfacqMYDLILSY-DKEDDlqpldlVPNNQGLTPFKLA 219
PHA03100 PHA03100
ankyrin repeat protein; Provisional
212-390 1.64e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  212 KMIKSKTEYPLHKAIK-VEREDVVFLYLIemdSQLPGKLNEADHNGDLALDLALSRRLES--IATTLVSHKADVDMVDKS 288
Cdd:PHA03100   64 STKNNSTPLHYLSNIKyNLTDVKEIVKLL---LEYGANVNAPDNNGITPLLYAISKKSNSysIVEYLLDNGANVNIKNSD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  289 GWSLLH---KGIQRgDLFAATFLIKNGAFVNAAT-------LGAQ--------ETPLHLVALYSSKkhsadvmsemaQIA 350
Cdd:PHA03100  141 GENLLHlylESNKI-DLKILKLLIDKGVDINAKNrvnyllsYGVPinikdvygFTPLHYAVYNNNP-----------EFV 208
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 110815813  351 EALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCK 390
Cdd:PHA03100  209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
PHA03100 PHA03100
ankyrin repeat protein; Provisional
901-1079 2.23e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  901 RVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQ-----DLPTICSVLLENGVDFAAVDENGNN 975
Cdd:PHA03100   29 DYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGIT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  976 ALHLAVMHgRLNNIRV--LLTECTVDAEAFNLRGQSPLHILGQYGKE---------------NAAAIFDLFLECmpGYPL 1038
Cdd:PHA03100  109 PLLYAISK-KSNSYSIveYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdiNAKNRVNYLLSY--GVPI 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 110815813 1039 DKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGV 1079
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
476-568 1.80e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.81  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   476 FLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQgANPNLQTEEalplpkeaasltsladsvhlQTPLHMAIAYNH 555
Cdd:pfam12796   15 LLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG--------------------RTALHYAARSGH 73
                           90
                   ....*....|...
gi 110815813   556 PDVVSVILEQKAN 568
Cdd:pfam12796   74 LEIVKLLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
342-411 4.46e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 4.46e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   342 VMSEMAQIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLDLelkDHEGSTALWLAVQH 411
Cdd:pfam12796    5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARS 71
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
770-799 3.52e-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: 3.52e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 110815813    770 DGQTPLHLAASWGLEETVQCLLEFGANVNA 799
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
829-982 4.75e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 4.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   829 IHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQvdnkGRNFLHVAVQNsdIESVLFLISVHANVNSRVQDASKL 908
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLE--YVDAVEAILLHLLAAFRKSGPLEL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   909 -------------TPLHLAVQAGSEIIVRNLLLAGAKV------NELTK--------HRQTALHLAAQQDLPTICSVLLE 961
Cdd:TIGR00870  117 andqytseftpgiTALHLAAHRQNYEIVKLLLERGASVparacgDFFVKsqgvdsfyHGESPLNAAACLGSPSIVALLSE 196
                          170       180
                   ....*....|....*....|.
gi 110815813   962 NGVDFAAVDENGNNALHLAVM 982
Cdd:TIGR00870  197 DPADILTADSLGNTLLHLLVM 217
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
167-235 3.04e-04

BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are separated by as little as two residues.


Pssm-ID: 197943 [Multi-domain]  Cd Length: 101  Bit Score: 41.17  E-value: 3.04e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813    167 CIRFYQTAEELNASTLMNYCAEIIASHWDDLRK-EDFSSMSAQLLYKMIKSKTeyplhkaIKVEREDVVF 235
Cdd:smart00875    1 CLGIRRFADAHGLEELAEKALRFILQNFSEVSSsEEFLELPLEQLLELLSSDD-------LNVSSEEEVF 63
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
289-408 1.34e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  289 GWSLLHKGIQRGDLFAATFLIKNGAFVNAATLGA------------QETPLHLVALYSSKkhsadvmsemaQIAEALLQA 356
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgnlfyfGELPLSLAACTNQE-----------EIVRLLLEN 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  357 GANP---NMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLDL---------------ELKDHEGSTALWLA 408
Cdd:cd21882   142 GAQPaalEAQDSLGNTVLHALVLQADNTPENSAFVCQMYNLllsygahldptqqleEIPNHQGLTPLKLA 211
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
491-519 5.54e-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: 35.64  E-value: 5.54e-03
                            10        20
                    ....*....|....*....|....*....
gi 110815813    491 GETPLHTACRHGLANLTAELLQQGANPNL 519
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
BTB_POZ_Rank-5 cd18303
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
50-169 5.05e-66

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1) or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms. It contains an N-terminal BTB domain, followed by a BACK domain, several ankyrin (ANK) repeats and a C-terminal FYVE domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349612 [Multi-domain]  Cd Length: 120  Bit Score: 217.96  E-value: 5.05e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   50 FISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFR 129
Cdd:cd18303     1 FISRLLKTVASLFDKELYSDITIKLADKSIPAHKFVLAARSEKWSNENLASTNELDLSDISYEVVLALLRWLYTDELDLT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 110815813  130 EDDVFLTELMKLANRFQLQLLRERCEKGVMSLVNVRNCIR 169
Cdd:cd18303    81 LDDEFLLELMKAAKRFQLTDLVERCERALMSSVNVDNCIR 120
BACK_ANKFY1_Rank5 cd18501
BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ...
162-250 1.02e-53

BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1), or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms.


Pssm-ID: 350576  Cd Length: 89  Bit Score: 181.68  E-value: 1.02e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  162 VNVRNCIRFYQTAEELNASTLMNYCAEIIASHWDDLRKEDFSSMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEM 241
Cdd:cd18501     1 VNVRNCIRFYQTAEEIGASTLREYCSEIISTHWDDLTPEDFAKMSAPLLYRMFKSKTKHPLHAAIRLKREDVVFLYLIEF 80

                  ....*....
gi 110815813  242 DSQLPGKLN 250
Cdd:cd18501    81 DSQLPGKLN 89
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
1102-1164 1.23e-46

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 160.67  E-value: 1.23e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815813 1102 EPPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1164
Cdd:cd15728     1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
639-977 3.27e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 3.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  639 LFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcw 718
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  719 gpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVN 798
Cdd:COG0666    82 --AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR------------DKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  799 AQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHV 878
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETP----------------------------------LHL 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  879 AVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSV 958
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVN--AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 110815813  959 LLENGVDFAAVDENGNNAL 977
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
790-1078 2.46e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 2.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  790 LLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVD 869
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  870 NKGRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQ 949
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVN--ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  950 QDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPLHILGQYGKENAAAIFDLF 1029
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 110815813 1030 LEcmpgyPLDKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQG 1078
Cdd:COG0666   242 GA-----DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
569-875 2.01e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 2.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  569 ALHATNNLQIIPDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADI 648
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  649 NVsRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATCWGPGpggcLQT 728
Cdd:COG0666    81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND----GNT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  729 LLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPI 808
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNAR------------DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813  809 HVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVDNKGRNF 875
Cdd:COG0666   224 DLAAENGNLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
604-908 8.44e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.67  E-value: 8.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  604 IAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRtQDGETALQLAIRNQLPLVVDAICTRGADMS 683
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALAD-ALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  684 VPDEKGNPPLWLALANNLEDIASTLVRHGCDATcwgpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgange 763
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  764 geeeARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPFA 843
Cdd:COG0666   150 ----DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALD 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813  844 CAMTFKNNKSAEAILKREsGAAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKL 908
Cdd:COG0666   225 LAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
434-705 4.67e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 4.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  434 FDENSFAARLIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQ 513
Cdd:COG0666    30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  514 GANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVL 593
Cdd:COG0666   110 GADVNARDKDG-------------------ETPLHLAAYNGNLEIVKLLLEAGA-------------DVNAQDNDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  594 GLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAIRNQLPLVVD 673
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVK 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 110815813  674 AICTRGADMSVPDEKGNPPLWLALANNLEDIA 705
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
1103-1164 2.10e-25

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 100.20  E-value: 2.10e-25
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813   1103 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1164
Cdd:smart00064    2 PHWIPDEEvsnCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDCYENL 66
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
1105-1164 5.22e-25

FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.


Pssm-ID: 277260 [Multi-domain]  Cd Length: 61  Bit Score: 99.00  E-value: 5.22e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813 1105 WCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1164
Cdd:cd15720     2 WKDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFGIEKEVRVCDPCYEKL 61
PHA03095 PHA03095
ankyrin-like protein; Provisional
698-994 1.62e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 105.49  E-value: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  698 ANNLEDIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNEpTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHL 777
Cdd:PHA03095   23 SNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD-IVRLLLEAGADVNAP------------ERCGFTPLHL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  778 AASWGLEETV-QCLLEFGANVNAQDAEGRTPIHVAISSQ--HGVIIQLLVSHpDIHLNVRDRQGLTPFACAMtfKNNKSA 854
Cdd:PHA03095   90 YLYNATTLDViKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRK-GADVNALDLYGMTPLAVLL--KSRNAN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  855 EAILKR--ESGAAE-QVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAVQAGS--EIIVRNLLLA 929
Cdd:PHA03095  167 VELLRLliDAGADVyAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIA 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813  930 GAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHgrlNNIRVLLT 994
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN---NNGRAVRA 308
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
1103-1165 4.64e-23

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 93.60  E-value: 4.64e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813  1103 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPII-KFDLNKPVRVCNICFDVLT 1165
Cdd:pfam01363    1 PVWVPDSSatvCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpELGSNKPVRVCDACYDTLQ 67
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
204-555 2.89e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 2.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  204 SMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEMDSQLPGKLNEADHNGDLALDLALSRRLESIATTLVSHKADVD 283
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  284 MVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNaATLGAQETPLHLVALYSSKKhsadvmsemaqIAEALLQAGANPNMQ 363
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLE-----------IVKLLLEAGADVNAQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  364 DSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLELKDHEGSTALWLAVQHitvssdqsvnpfEDVPVVNgtsfdensfaarl 443
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAEN------------GHLEIVK------------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  444 iqrgshtdapdtatgncllqraagagneaaalFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEE 523
Cdd:COG0666   204 --------------------------------LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
                         330       340       350
                  ....*....|....*....|....*....|..
gi 110815813  524 ALPLPKEAASLTSLADSVHLQTPLHMAIAYNH 555
Cdd:COG0666   252 GLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
178-411 8.14e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 8.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  178 NASTLMNYCAEIIASHWDDLRKEDFSSMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEMDSqlpgkLNEADHNGD 257
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD-----INAKDDGGN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  258 LALDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNAATlGAQETPLHLVALYSSKK 337
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLE 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110815813  338 hsadvmsemaqIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLELKDHEGSTALWLAVQH 411
Cdd:COG0666   168 -----------IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE-AGADVNAKDNDGKTALDLAAEN 229
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
435-693 1.09e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  435 DENSFAARLIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQG 514
Cdd:COG0666    64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  515 ANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLG 594
Cdd:COG0666   144 ADVNAQDNDG-------------------NTPLHLAAANGNLEIVKLLLEAGA-------------DVNARDNDGETPLH 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  595 LALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAIRNQLPLVVDA 674
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA-KDKDGLTALLLAAAAGAALIVKL 270
                         250
                  ....*....|....*....
gi 110815813  675 ICTRGADMSVPDEKGNPPL 693
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
503-823 3.61e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.41  E-value: 3.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  503 LANLTAELLQQGANPNLQTEEALPLPKEAASLTSLADSVHLQTPLHMAIAYNHPDVVSVILEQKANALHATNNLQIIPDF 582
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  583 SLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQL 662
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  663 AIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcwgpgpggclqtllhrAIDENnepta 742
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN----------------AKDND----- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  743 cflirsgcdvnsprqpgangegeeeardGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQL 822
Cdd:COG0666   219 ----------------------------GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                  .
gi 110815813  823 L 823
Cdd:COG0666   271 L 271
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
1111-1161 1.89e-20

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 85.66  E-value: 1.89e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110815813 1111 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1161
Cdd:cd00065     2 CMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSGKPVRVCDSCY 52
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
236-575 4.01e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.32  E-value: 4.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  236 LYLIEMDSQLPGKLNEADHNGDLALDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLIKNGAFV 315
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  316 NAATLGaQETPLHLVALYSSKKhsadvmsemaqIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLE 395
Cdd:COG0666    81 NAKDDG-GNTLLHAAARNGDLE-----------IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  396 LKDHEGSTALWLAVQHitvssdqsvnpfEDVPVVNgtsfdensfaarliqrgshtdapdtatgncllqraagagneaaal 475
Cdd:COG0666   148 AQDNDGNTPLHLAAAN------------GNLEIVK--------------------------------------------- 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  476 FLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNH 555
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG-------------------KTALDLAAENGN 231
                         330       340
                  ....*....|....*....|
gi 110815813  556 PDVVSVILEQKANALHATNN 575
Cdd:COG0666   232 LEIVKLLLEAGADLNAKDKD 251
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
1103-1161 3.55e-19

FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.


Pssm-ID: 277274 [Multi-domain]  Cd Length: 59  Bit Score: 82.19  E-value: 3.55e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 110815813 1103 PPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1161
Cdd:cd15735     1 PEWVDSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQPVRVCDGCY 59
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
1102-1162 3.65e-19

FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.


Pssm-ID: 277270 [Multi-domain]  Cd Length: 65  Bit Score: 82.39  E-value: 3.65e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813 1102 EPP-W---CDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFD 1162
Cdd:cd15731     1 DPPlWvpdEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGQMKPVRVCNHCFM 65
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
1103-1164 1.64e-18

FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.


Pssm-ID: 277269 [Multi-domain]  Cd Length: 63  Bit Score: 80.52  E-value: 1.64e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813 1103 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlnKPVRVCNICFDVL 1164
Cdd:cd15730     1 RKWADDEEvqnCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSK--KPVRVCDACFDDL 63
PHA02876 PHA02876
ankyrin repeat protein; Provisional
788-1012 3.28e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 90.12  E-value: 3.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  788 QCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAaeq 867
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI--- 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  868 vdNKGRNFLHVAVQNSDIESVLFLISVHANVNSrvQDASKLTPLHLAVQAGS-EIIVRNLLLAGAKVNELTKHRQTALHL 946
Cdd:PHA02876  238 --NKNDLSLLKAIRNEDLETSLLLYDAGFSVNS--IDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYL 313
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813  947 AAQQDLPTI-CSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAEAFNLRGQSPLH 1012
Cdd:PHA02876  314 MAKNGYDTEnIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIH 380
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
854-1084 5.07e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.16  E-value: 5.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  854 AEAILKRESGAAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKV 933
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  934 NELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPLHI 1013
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110815813 1014 LGQYGKEnaaAIFDLFLECmpGYPLDKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGVNIFNY 1084
Cdd:COG0666   160 AAANGNL---EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
1102-1160 6.02e-18

FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.


Pssm-ID: 277266 [Multi-domain]  Cd Length: 64  Bit Score: 78.96  E-value: 6.02e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110815813 1102 EPPW---CDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNIC 1160
Cdd:cd15727     1 EPPWvpdKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPRMCFVDPVRVCNEC 62
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
1108-1164 1.33e-17

FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.


Pssm-ID: 277259 [Multi-domain]  Cd Length: 65  Bit Score: 77.81  E-value: 1.33e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813 1108 GSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1164
Cdd:cd15719     9 GDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRISRPVRVCQACYNIL 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
785-1079 3.43e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 3.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  785 ETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV---IIQLLVSHpDIHLNVRDRQGLTPFACAMTFKNnksAEAILKR- 860
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEA-GADVNAPERCGFTPLHLYLYNAT---TLDVIKLl 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  861 -ESGA-AEQVDNKGRNFLHV--AVQNSDIESVLFLISVHANVNSRvqDASKLTPLH-LAVQAGSEI-IVRNLLLAGAKVN 934
Cdd:PHA03095  104 iKAGAdVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNAL--DLYGMTPLAvLLKSRNANVeLLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  935 ELTKHRQTALHLAAQ--QDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRvlltectvdaeafnlrgqsplh 1012
Cdd:PHA03095  182 AVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSL---------------------- 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813 1013 ilgqygkenaaaIFDLFLEcmpGYPLDKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGV 1079
Cdd:PHA03095  240 ------------VLPLLIA---GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
67-145 4.64e-17

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing (ZBTB) proteins, Kelch-like (KLHL) proteins, and similar proteins; This family includes a variety of BTB/POZ domain-containing proteins, such as zinc finger and BTB domain-containing (ZBTB) proteins and Kelch-like (KLHL) proteins. They have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349497 [Multi-domain]  Cd Length: 82  Bit Score: 76.82  E-value: 4.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   67 YSDLKIKVGDRHISAHKFVLAARSD-----SWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVFltELMKL 141
Cdd:cd18186     1 LCDVTLVVGGREFPAHRAVLAARSPyframFSSGMKESSSSEIELDDVSPEAFEALLDYIYTGELELSEENVE--ELLAA 78

                  ....
gi 110815813  142 ANRF 145
Cdd:cd18186    79 ADKL 82
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
1109-1161 5.05e-17

FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.


Pssm-ID: 277272 [Multi-domain]  Cd Length: 60  Bit Score: 76.32  E-value: 5.05e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110815813 1109 SYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1161
Cdd:cd15733     8 SHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQLYDPVRVCNSCY 60
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
1104-1161 1.09e-16

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.


Pssm-ID: 277299 [Multi-domain]  Cd Length: 59  Bit Score: 75.03  E-value: 1.09e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 110815813 1104 PWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKF-DLNKPVRVCNICF 1161
Cdd:cd15760     1 HWKPDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPHLgPLGVPQRVCDRCF 59
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
69-156 1.11e-16

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 76.58  E-value: 1.11e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813     69 DLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELD-----LSDANPEVTMTMLRWIYTDELEFREDDVFltELMKLAN 143
Cdd:smart00225    1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDkseiyLDDVSPEDFRALLNFLYTGKLDLPEENVE--ELLELAD 78
                            90
                    ....*....|...
gi 110815813    144 RFQLQLLRERCEK 156
Cdd:smart00225   79 YLQIPGLVELCEE 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
624-829 2.08e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  624 TLLHMAIQRQDSKSALFLLEHQADINVSRTQDgETAL-----QLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALA 698
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNN-STPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  699 NNLED--IASTLVRHGCDA---TCWGPGP------GGC-----LQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgang 762
Cdd:PHA03100  116 KKSNSysIVEYLLDNGANVnikNSDGENLlhlyleSNKidlkiLKLLIDKGVDINAKNRVNYLLSYGVPINIK------- 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  763 egeeearD--GQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSH-PDI 829
Cdd:PHA03100  189 -------DvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNgPSI 251
PHA02874 PHA02874
ankyrin repeat protein; Provisional
648-1006 2.09e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.09  E-value: 2.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  648 INVSrTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATCWgPGPggclq 727
Cdd:PHA02874   28 INIS-VDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL-PIP----- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  728 tllhraiDENNEpTACFLIRSGCDVNSprqpgangegeeEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTP 807
Cdd:PHA02874  101 -------CIEKD-MIKTILDCGIDVNI------------KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  808 IHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHVAVQNSDIES 887
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEK-GAYANVKDNNGESP----------------------------------LHNAAEYGDYAC 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  888 VLFLISVHANVNSRVQDAskLTPLHLAVQAGSEIIvrNLLLAGAKVNELTKHRQTALHLAAQQDLPT-ICSVLLENGVDF 966
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNG--FTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADI 281
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 110815813  967 AAVDENGNNALHLAVMH-GRLNNIRVLLTECTVDAEAFNLR 1006
Cdd:PHA02874  282 SIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADKLK 322
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
60-156 2.42e-16

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 75.76  E-value: 2.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813    60 DLYEQEQYSDLKIKVGDRHISAHKFVLAARSDS-WSLANL----SSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 134
Cdd:pfam00651    3 ELREQGELCDVTLVVGDKEFRAHKAVLAACSPYfKALFSGqeseSSVSEITLDDVSPEDFEALLEFMYTGKLISEENVD- 81
                           90       100
                   ....*....|....*....|..
gi 110815813   135 ltELMKLANRFQLQLLRERCEK 156
Cdd:pfam00651   82 --DLLAAADKLQIPSLVDKCEE 101
PHA02874 PHA02874
ankyrin repeat protein; Provisional
773-1017 3.06e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 3.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  773 TPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVshpdihLNVRDRQGLtPFACAmtfkNNK 852
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI------DNGVDTSIL-PIPCI----EKD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  853 SAEAILkrESGAAEQV-DNKGRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGA 931
Cdd:PHA02874  106 MIKTIL--DCGIDVNIkDAELKTFLHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  932 KVNELTKHRQTALHLAAQQ-DLPTIcSVLLENGVDFAAVDENGNNALHLAVMHGRlNNIRVLLTECTVDAEAFNlrGQSP 1010
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYgDYACI-KLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDID--GSTP 257

                  ....*..
gi 110815813 1011 LHILGQY 1017
Cdd:PHA02874  258 LHHAINP 264
BTB_POZ_trishanku-like cd18314
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
62-154 9.71e-16

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Dictyostelium discoideum trishanku and similar proteins; Trishanku is a novel regulator required for normal morphogenesis and cell-type stability in Dictyostelium discoideum. It contains a BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349623 [Multi-domain]  Cd Length: 96  Bit Score: 73.53  E-value: 9.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   62 YEQEQYSDLKIKVGDRHISAHKFVLAARSDSWS---LANL--SSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVFlt 136
Cdd:cd18314     1 YNDSEFSDVVLCVGDRKFFAHRIVLCARSPVFRsmlTGSMieSNLKEVTLEDVEPEIFETVLKYMYTGQVTLSEENVL-- 78
                          90
                  ....*....|....*...
gi 110815813  137 ELMKLANRFQLQLLRERC 154
Cdd:cd18314    79 DLLMLASKYQVPDLEKLC 96
PHA02876 PHA02876
ankyrin repeat protein; Provisional
604-1017 1.17e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.03  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  604 IAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSrTQDGETALQLAIRNQLPLVVDAICtrgadms 683
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNII-ALDDLSVLECAVDSKNIDTIKAII------- 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  684 vpDEKGNPplwlalanNLEDIAstlvrhgcdatcwgpgpggclqtlLHRAIDENNEPTACFLIRSGCDVNSPrqpgange 763
Cdd:PHA02876  232 --DNRSNI--------NKNDLS------------------------LLKAIRNEDLETSLLLYDAGFSVNSI-------- 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  764 geEEARDgqTPLHLAA-SWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV--IIQLLVSHPDIhlNVRDRQGLT 840
Cdd:PHA02876  270 --DDCKN--TPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTenIRTLIMLGADV--NAADRLYIT 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  841 PFACAMTFKNNKsaeailkresgaaeqvdnkgrnflhvavqnsdiESVLFLISVHANVNSRvqDASKLTPLHLAVQAGSE 920
Cdd:PHA02876  344 PLHQASTLDRNK---------------------------------DIVITLLELGANVNAR--DYCDKTPIHYAAVRNNV 388
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  921 IIVRNLLLAGAKVNELTKHRQTALHLAAQQDLP-TICSVLLENGVDFAAVDENGNNALHLAVMHG-RLNNIRVLLtECTV 998
Cdd:PHA02876  389 VIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLL-DNGA 467
                         410
                  ....*....|....*....
gi 110815813  999 DAEAFNLRGQSPLHILGQY 1017
Cdd:PHA02876  468 DVNAINIQNQYPLLIALEY 486
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
61-156 3.04e-15

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 19 (BTBD19); BTBD19 is a BTB domain-containing protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349603 [Multi-domain]  Cd Length: 111  Bit Score: 72.66  E-value: 3.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   61 LYEQEQYSDLKIKVGDR--HISAHKFVLAARSDSWS------LANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDD 132
Cdd:cd18294     8 LINNPEFSDVKFLVGPErqEIFAHKCILAARCEVFRamfltgPQKESTQSPLVLSDIEPEVFRAVLEFIYTNCVTLSNHT 87
                          90       100
                  ....*....|....*....|....
gi 110815813  133 VFltELMKLANRFQLQLLRERCEK 156
Cdd:cd18294    88 VI--EVLAAAVEYGLDELRKLCER 109
Ank_2 pfam12796
Ankyrin repeats (3 copies);
876-970 9.02e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 9.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   876 LHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRnLLLAGAKVNELTKHRqTALHLAAQQDLPTI 955
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDNGR-TALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 110815813   956 CSVLLENGVDFAAVD 970
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
1107-1165 9.76e-15

FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.


Pssm-ID: 277278 [Multi-domain]  Cd Length: 73  Bit Score: 70.06  E-value: 9.76e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 110815813 1107 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPiiKFDLNKPVRVCNICFDVLT 1165
Cdd:cd15739     9 DVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVP--SGPNRRPARVCDVCHTLLV 65
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
1111-1161 3.65e-14

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.


Pssm-ID: 277264 [Multi-domain]  Cd Length: 62  Bit Score: 68.12  E-value: 3.65e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110815813 1111 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1161
Cdd:cd15725    11 CYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCC 61
PHA02878 PHA02878
ankyrin repeat protein; Provisional
774-1013 4.69e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.07  E-value: 4.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  774 PLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVShpdihLNVRDRQGLTPFACAMTFKNNKS 853
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR-----SINKCSVFYTLVAIKDAFNNRNV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  854 --AEAILKRESGAAEQVDNKgrnFLHVAVQNSDIES--VLFLISVHANVNSRVQDASKlTPLHLAVQAGSEIIVRNLLLA 929
Cdd:PHA02878  115 eiFKIILTNRYKNIQTIDLV---YIDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSY 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  930 GAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVmhGRLNNIRVL--LTECTVDAEAFN-LR 1006
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKDYDILklLLEHGVDVNAKSyIL 268

                  ....*..
gi 110815813 1007 GQSPLHI 1013
Cdd:PHA02878  269 GLTALHS 275
Ank_2 pfam12796
Ankyrin repeats (3 copies);
775-901 6.33e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 6.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   775 LHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIhlnvrdrqgltpfacamtfknnksa 854
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV------------------------- 55
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 110815813   855 eailkresgaaeQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSR 901
Cdd:pfam12796   56 ------------NLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
1111-1161 6.38e-14

FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277261 [Multi-domain]  Cd Length: 58  Bit Score: 67.41  E-value: 6.38e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110815813 1111 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFdlNKPVRVCNICF 1161
Cdd:cd15721    10 CQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSS--AKPVRVCDTCY 58
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
1111-1161 1.41e-13

FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.


Pssm-ID: 277271 [Multi-domain]  Cd Length: 61  Bit Score: 66.46  E-value: 1.41e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110815813 1111 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1161
Cdd:cd15732    11 CYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQLFEPSRVCKSCF 61
Ank_2 pfam12796
Ankyrin repeats (3 copies);
911-993 1.51e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 1.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   911 LHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSVLLENGvdFAAVDENGNNALHLAVMHGRLNNIR 990
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGHLEIVK 78

                   ...
gi 110815813   991 VLL 993
Cdd:pfam12796   79 LLL 81
FYVE_WDFY1_like cd15718
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ...
1103-1161 1.56e-13

FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins; This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats.


Pssm-ID: 277258 [Multi-domain]  Cd Length: 70  Bit Score: 66.58  E-value: 1.56e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110815813 1103 PPWCDGSYCYECTARF-----------GVTTRKHHCRHCGRLLCHKCSTKE--IPIIKFDLnkPVRVCNICF 1161
Cdd:cd15718     1 PEWAESDNCQKCSRPFfwnfkqmwekkTLGVRQHHCRKCGKAVCDKCSSNRstIPVMGFEF--PVRVCNECY 70
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
1107-1164 1.62e-13

FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277297 [Multi-domain]  Cd Length: 71  Bit Score: 66.63  E-value: 1.62e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 110815813 1107 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlnKPVRVCNICFDVL 1164
Cdd:cd15758    11 EATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYP--KPVRVCDSCHTLL 66
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
1101-1164 1.74e-13

FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.


Pssm-ID: 277268 [Multi-domain]  Cd Length: 68  Bit Score: 66.22  E-value: 1.74e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110815813 1101 KEPP-WC---DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTkeipiIKFDL----NKPVRVCNICFDVL 1164
Cdd:cd15729     2 KVAPvWVpdsEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCS-----LKARLeyldNKEARVCVPCYQTL 68
PHA02875 PHA02875
ankyrin repeat protein; Provisional
767-965 1.01e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.56  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  767 EARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFACAM 846
Cdd:PHA02875   31 EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLAT 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  847 TFKNNKSAEAILKResGAAEQVDNKGR-NFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRN 925
Cdd:PHA02875  111 ILKKLDIMKLLIAR--GADPDIPNTDKfSPLHLAVMMGDIKGIELLIDHKACLD--IEDCCGCTPLIIAMAKGDIAICKM 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 110815813  926 LLLAGAKVNELTKHRQ-TALHLAAQQDLPTICSVLLENGVD 965
Cdd:PHA02875  187 LLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
587-889 1.02e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  587 SRDQTVLGL--ALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRTQDgetalqlaI 664
Cdd:PHA02874   31 SVDETTTPLidAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPC--------I 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  665 RNQLplvVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATCwgPGPGGCLQtlLHRAIDENNEPTACF 744
Cdd:PHA02874  103 EKDM---IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI--EDDNGCYP--IHIAIKHNFFDIIKL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  745 LIRSGCDVNSprqpgangegeeEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIiQLLV 824
Cdd:PHA02874  176 LLEKGAYANV------------KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI-ELLI 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813  825 SHPDIhlNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVDNKGRNFLHVAVQNSDIESVL 889
Cdd:PHA02874  243 NNASI--NDQDIDGSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVI 305
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
1111-1161 1.36e-12

FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.


Pssm-ID: 277273 [Multi-domain]  Cd Length: 61  Bit Score: 63.51  E-value: 1.36e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110815813 1111 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1161
Cdd:cd15734    11 CSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHPVRVCDPCA 61
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
1111-1161 1.45e-12

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277257 [Multi-domain]  Cd Length: 61  Bit Score: 63.54  E-value: 1.45e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 110815813 1111 CYECT-ARFGVTTRKHHCRHCGRLLCHKCSTKeipiiKFDL----NKPVRVCNICF 1161
Cdd:cd15717    11 CMHCKkTKFTAINRRHHCRKCGAVVCGACSSK-----KFLLphqsSKPLRVCDTCY 61
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
1111-1164 2.15e-12

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway.


Pssm-ID: 277293 [Multi-domain]  Cd Length: 64  Bit Score: 63.05  E-value: 2.15e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813 1111 CYECT-ARFGVTTRKHHCRHCGRLLCHKCSTKE--IPIIKfdlNKPVRVCNICFDVL 1164
Cdd:cd15754    11 CMRCTqTNFSLLTRRHHCRKCGFVVCHECSRQRflIPRLS---PKPVRVCSLCYRKL 64
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
1104-1161 2.17e-12

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.


Pssm-ID: 277282 [Multi-domain]  Cd Length: 61  Bit Score: 62.84  E-value: 2.17e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 110815813 1104 PWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlNKPVRVCNICF 1161
Cdd:cd15743     5 PDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPLEYLK-NKSARVCDECF 61
PHA02876 PHA02876
ankyrin repeat protein; Provisional
477-823 6.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  477 LATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEALplpkeaasltsladsvhlqTPLHMAIAYNHP 556
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDL-------------------SVLECAVDSKNI 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  557 DVVSVILEQKANA-------LHATNNLQIIPDFSLKDSR---------DQTVLGLALWT-GMHTIAAQLLGSGAAINDTM 619
Cdd:PHA02876  225 DTIKAIIDNRSNInkndlslLKAIRNEDLETSLLLYDAGfsvnsiddcKNTPLHHASQApSLSRLVPKLLERGADVNAKN 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  620 SDGQTLLH-MAIQRQDSKSALFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALA 698
Cdd:PHA02876  305 IKGETPLYlMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAV 384
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  699 NNLEDIASTLVRHGCDATCWGPGPGgclqTLLHRAIDENNEPTAC-FLIRSGCDVNSprqpgangegeeEARDGQTPLHL 777
Cdd:PHA02876  385 RNNVVIINTLLDYGADIEALSQKIG----TALHFALCGTNPYMSVkTLIDRGANVNS------------KNKDLSTPLHY 448
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 110815813  778 AASWGLE-ETVQCLLEFGANVNAQDAEGRTPIHVAIsSQHGVIIQLL 823
Cdd:PHA02876  449 ACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL-EYHGIVNILL 494
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
1104-1164 1.13e-11

FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins; Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP).


Pssm-ID: 277256 [Multi-domain]  Cd Length: 61  Bit Score: 60.82  E-value: 1.13e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110815813 1104 PWCDGS---YCYECTARFGVTTRKHHCRHCGRLLCHKCStkeipiiKFdLNKPVRVCNICFDVL 1164
Cdd:cd15716     3 PWVNDSdvpFCPDCGKKFNLARRRHHCRLCGSIMCNKCS-------QF-LPLHIRCCHHCKDLL 58
BTB2_POZ_RhoBTB cd18300
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
67-155 1.46e-11

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing proteins (RhoBTB); RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, a tandem of 2 BTB domains, and a conserved C-terminal region. In humans, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349609 [Multi-domain]  Cd Length: 108  Bit Score: 62.26  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   67 YSDLKIKVGDRHISAHKFVLAARSDsWSLANL------SSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVFLtELMK 140
Cdd:cd18300     9 FSDVTFIVEDGTIPAHKALLVARCD-VMAAMFggnfreSSAKEVELPGVSKETFLALLEYLYTDQAPILEDGDCV-GLIV 86
                          90
                  ....*....|....*
gi 110815813  141 LANRFQLQLLRERCE 155
Cdd:cd18300    87 LANRLCLPRLVALCE 101
PHA03100 PHA03100
ankyrin repeat protein; Provisional
728-972 1.53e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.77  E-value: 1.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  728 TLLHRAIDENNEPTACFLIRSGCDVNSprqpgangegeeEARDGQTPLHLAASWGLE-----ETVQCLLEFGANVNAQDA 802
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINS------------STKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  803 EGRTPIHVAIS--SQHGVIIQLLVSHpdihlnvrdrqgltpfACAMTFKNNKsaeailkresgaaeqvdnkGRNFLHVAV 880
Cdd:PHA03100  105 NGITPLLYAISkkSNSYSIVEYLLDN----------------GANVNIKNSD-------------------GENLLHLYL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  881 QNSDIES--VLFLISVHANVNSR--------------VQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTAL 944
Cdd:PHA03100  150 ESNKIDLkiLKLLIDKGVDINAKnrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
                         250       260
                  ....*....|....*....|....*...
gi 110815813  945 HLAAQQDLPTICSVLLENGVDFAAVDEN 972
Cdd:PHA03100  230 HIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
307-580 1.75e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  307 FLIKNGAFVNAATL-GAqeTPLHLVALYSSKkhsADVMsemaqiaEALLQAGANPNMQDSKGRTPLHV--SIMAGNEYVF 383
Cdd:PHA03095   68 LLLEAGADVNAPERcGF--TPLHLYLYNATT---LDVI-------KLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  384 SQLLQcKQLDLELKDHEGSTALwlavqHITVSS------------DQSVNPFeDVPVVNGTSFDE--NSFAAR------L 443
Cdd:PHA03095  136 RLLLR-KGADVNALDLYGMTPL-----AVLLKSrnanvellrlliDAGADVY-AVDDRFRSLLHHhlQSFKPRarivreL 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  444 IQRGSHTDAPDtATGNCLLQRAAGAGNEAAAL---FLAtNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQ 520
Cdd:PHA03095  209 IRAGCDPAATD-MLGNTPLHSMATGSSCKRSLvlpLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813  521 TEEALplpkeaasltsladsvhlqTPLHMAIAYNHPDVVSVILEQK------ANAL-HATNNLQIIP 580
Cdd:PHA03095  287 SSDGN-------------------TPLSLMVRNNNGRAVRAALAKNpsaetvAATLnTASVAGGDIP 334
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
1104-1164 2.91e-11

FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277294 [Multi-domain]  Cd Length: 64  Bit Score: 60.05  E-value: 2.91e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110815813 1104 PWCDGSYCYECT-ARFGVTTRKHHCRHCGRLLCHKCSTKEIpIIKFDLNKPVRVCNICFDVL 1164
Cdd:cd15755     4 PDSEATVCMRCQkAKFTPVNRRHHCRKCGFVVCGPCSEKKF-LLPSQSSKPVRVCDFCYDLL 64
FYVE2_Vac1p_like cd15737
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ...
1104-1160 3.14e-11

FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p.


Pssm-ID: 277276 [Multi-domain]  Cd Length: 83  Bit Score: 60.60  E-value: 3.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813 1104 PWCDGS---YCYECTARFGVTTRKHHCRHCGRLLCH----KCSTkEIPI--------------IKFDLNKP-----VRVC 1157
Cdd:cd15737     1 PWEDDSsvtHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCST-EVPLdllssalpdlpfvfKEPQSDIPddtksVRVC 79

                  ...
gi 110815813 1158 NIC 1160
Cdd:cd15737    80 RDC 82
PHA03100 PHA03100
ankyrin repeat protein; Provisional
867-1034 3.15e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 3.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  867 QVDNKGRNFLH-----VAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQA--GSEIIVRNLLLAGAKVNELTKH 939
Cdd:PHA03100   63 SSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN--APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  940 RQTALHLAAQQDLPT--ICSVLLENGVDFAA----------------VDENGNNALHLAVMHGRLNNIRVLLtECTVDAE 1001
Cdd:PHA03100  141 GENLLHLYLESNKIDlkILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPN 219
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 110815813 1002 AFNLRGQSPLH--ILGQYGkenaaAIFDLFLECMP 1034
Cdd:PHA03100  220 LVNKYGDTPLHiaILNNNK-----EIFKLLLNNGP 249
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
1111-1164 4.73e-11

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4; This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity.


Pssm-ID: 277280 [Multi-domain]  Cd Length: 65  Bit Score: 59.42  E-value: 4.73e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110815813 1111 CYECTARF-GVTTRKHHCRHCGRLLCHKCSTKEIPiIKFDLNKPVRVCNICFDVL 1164
Cdd:cd15741    12 CMRCKEPFnALTRRRHHCRACGYVVCWKCSDYKAT-LEYDGNKLNRVCKHCYVIL 65
FYVE_WDFY1 cd15756
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ...
1103-1164 5.22e-11

FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.


Pssm-ID: 277295 [Multi-domain]  Cd Length: 76  Bit Score: 59.70  E-value: 5.22e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813 1103 PPWCDGSYCYECTARF-----------GVTTRKHHCRHCGRLLCHKCSTKE--IPIIKFDLNkpVRVCNICFDVL 1164
Cdd:cd15756     1 PQWLESDSCQKCEQPFfwnikqmwdtkTLGLRQHHCRKCGQAVCGKCSSKRssYPIMGFEFQ--VRVCDSCFETI 73
Ank_2 pfam12796
Ankyrin repeats (3 copies);
944-1023 7.56e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 7.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   944 LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAeafNLRGQSPLHILGQYGKENAA 1023
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
PHA02878 PHA02878
ankyrin repeat protein; Provisional
546-826 9.35e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 9.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  546 PLHMAIAYNHPDVVSVILEQKANA----------LH----ATNNLQIIPDFSLKDSRDQTVLGLALWTGMHT----IAAQ 607
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVnqpdhrdltpLHiickEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNrnveIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  608 LLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDE 687
Cdd:PHA02878  120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  688 KGNPPLWLALANNLEDIASTLVRHGCDATCwgpgPGGCLQTLLHRAIDE-NNEPTACFLIRSGCDVNSprqpgangegeE 766
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDA----RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNA-----------K 264
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110815813  767 EARDGQTPLHLAASwgLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV-IIQLLVSH 826
Cdd:PHA02878  265 SYILGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCInIGRILISN 323
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
727-845 1.12e-10

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: 65.80  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  727 QTLLHRAIDENNEPTACFLIRSGCDVNSPRqpgANGEGEEEARD-----GQTPLHLAASWGLEETVQCLLEFGANVNAQD 801
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVSPR---ATGTFFRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 110815813  802 AEGRTPIHVAISSQHGV----IIQLLVSHpDIHLN------VRDRQGLTPFACA 845
Cdd:cd22192   167 SLGNTVLHILVLQPNKTfacqMYDLILSY-DKEDDlqpldlVPNNQGLTPFKLA 219
PHA02876 PHA02876
ankyrin repeat protein; Provisional
349-714 1.14e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.86  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  349 IAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQlDLELKDHEGSTALWLAVQHITVSSDQSVnpfedvpV 428
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA-DVNIIALDDLSVLECAVDSKNIDTIKAI-------I 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  429 VNGTSFDENSFAarLIQRGSHTDAPDTatgncllqraagagneaaaLFLATNGAHVNHRNKWGETPLHTACRH-GLANLT 507
Cdd:PHA02876  232 DNRSNINKNDLS--LLKAIRNEDLETS-------------------LLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLV 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  508 AELLQQGANPNLQ-----------------TEEALPLPKEAASLTSlADSVHLqTPLHMAIAYN-HPDVVSVILEQKANA 569
Cdd:PHA02876  291 PKLLERGADVNAKnikgetplylmakngydTENIRTLIMLGADVNA-ADRLYI-TPLHQASTLDrNKDIVITLLELGANV 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  570 lhatnnlqiipdfSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDS-KSALFLLEHQADI 648
Cdd:PHA02876  369 -------------NARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANV 435
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813  649 NvSRTQDGETALQLAIRNQL-PLVVDAICTRGADMSVPDEKGNPPLWLALAnnLEDIASTLVRHGCD 714
Cdd:PHA02876  436 N-SKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNAINIQNQYPLLIALE--YHGIVNILLHYGAE 499
BTB_POZ_BTBD9 cd18287
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
58-150 1.17e-10

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 9 (BTBD9); BTBD9 is a risk factor for Restless Legs Syndrome (RLS) encoding a Cullin-3 substrate adaptor. The BTBD9 gene may be associated with antipsychotic-induced RLS in schizophrenia. Mutations in BTBD9 lead to reduced dopamine, increased locomotion and sleep fragmentation. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349596 [Multi-domain]  Cd Length: 119  Bit Score: 59.94  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   58 VADLYEQEQYSDLKIKVGDRHISAHKFVLAARSdSWSLANL------SSTKELDLSDANPEVTMTMLRWIYTDELEFR-- 129
Cdd:cd18287    13 IGALFLNEEYSDVTFVVEEKRFPAHRVILAARS-EYFRALLyggmreSQQSEIELKDTNAEAFKALLKYIYTGRLTLTdl 91
                          90       100
                  ....*....|....*....|.
gi 110815813  130 EDDVFLtELMKLANRFQLQLL 150
Cdd:cd18287    92 KEDVLL-DVLGLAHQYGFEEL 111
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
1109-1162 1.31e-10

FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.


Pssm-ID: 277263 [Multi-domain]  Cd Length: 61  Bit Score: 57.91  E-value: 1.31e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110815813 1109 SYCYECTA-RFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNkPVRVCNICFD 1162
Cdd:cd15724     8 SVCMVCQVeRFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYREN-PVRVCDQCYE 61
PHA03100 PHA03100
ankyrin repeat protein; Provisional
212-390 1.64e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  212 KMIKSKTEYPLHKAIK-VEREDVVFLYLIemdSQLPGKLNEADHNGDLALDLALSRRLES--IATTLVSHKADVDMVDKS 288
Cdd:PHA03100   64 STKNNSTPLHYLSNIKyNLTDVKEIVKLL---LEYGANVNAPDNNGITPLLYAISKKSNSysIVEYLLDNGANVNIKNSD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  289 GWSLLH---KGIQRgDLFAATFLIKNGAFVNAAT-------LGAQ--------ETPLHLVALYSSKkhsadvmsemaQIA 350
Cdd:PHA03100  141 GENLLHlylESNKI-DLKILKLLIDKGVDINAKNrvnyllsYGVPinikdvygFTPLHYAVYNNNP-----------EFV 208
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 110815813  351 EALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCK 390
Cdd:PHA03100  209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
1107-1164 2.16e-10

FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions.


Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 57.73  E-value: 2.16e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 110815813 1107 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlnKPVRVCNICFDVL 1164
Cdd:cd15759     9 EATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSP--KPVRVCDSCHAML 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
770-832 3.71e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.15  E-value: 3.71e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815813  770 DGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIHLN 832
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
BTB_POZ_KLHL7 cd18237
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
61-168 4.03e-10

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 7 (KLHL7); KLHL7 is a component of a Cul3-based E3 ubiquitin ligase complex and is involved in the ubiquitination of target proteins for proteasome-mediated degradation. Mutations in KLHL7 causes autosomal-dominant retinitis pigmentosa. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349546 [Multi-domain]  Cd Length: 126  Bit Score: 58.65  E-value: 4.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   61 LYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSL---ANL--SSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVfl 135
Cdd:cd18237    15 MRKQKTLCDVILIVEGREIKAHRVVLAAASHFFHLmftSNMteSKSSEVELKDAEPDIIELLVEFAYTARISVNSNNV-- 92
                          90       100       110
                  ....*....|....*....|....*....|...
gi 110815813  136 TELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18237    93 QSLLDAANQYQIEPVKKMCVDFLKEQLDASNCL 125
PHA02875 PHA02875
ankyrin repeat protein; Provisional
769-899 4.43e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.09  E-value: 4.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  769 RDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIhLNVRDRQGLTPFACAMTF 848
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAK 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110815813  849 KNNKSAEAILkrESGAaeQVDNKGRN----FLHVAVQNSDIESVLFLISVHANVN 899
Cdd:PHA02875  179 GDIAICKMLL--DSGA--NIDYFGKNgcvaALCYAIENNKIDIVRLFIKRGADCN 229
BTB_POZ_SPOPL cd18343
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
53-166 5.00e-10

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein-like (SPOPL); SPOPL, also called HIB homolog 2 or Roadkill homolog 2, is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The complexes may contain homodimeric SPOPL or the heterodimers formed by speckle-type POZ protein (SPOP) and SPOPL, which are less efficient than ubiquitin ligase complexes containing only SPOP. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349652 [Multi-domain]  Cd Length: 123  Bit Score: 58.48  E-value: 5.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   53 RLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSL-----ANLSSTKELDLSDANPEVTMTMLRWIYTDE-- 125
Cdd:cd18343     7 RLAEDLGNLWENSRFTDCSLFVGGQEFKAHKSILAARSPVFNAmfeheMEESKKNRVEINDVDPEVFKEMMRFIYTGKap 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 110815813  126 -LEFREDDvflteLMKLANRFQLQLLRERCEKGVMSLVNVRN 166
Cdd:cd18343    87 nLDKMADN-----LLAAADKYALERLKVMCEEALCNNLSVEN 123
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
1111-1161 5.41e-10

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 55.97  E-value: 5.41e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110815813 1111 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1161
Cdd:cd15745     2 CAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVPDTCIYLRVCKTCY 52
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
1111-1161 5.76e-10

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277281 [Multi-domain]  Cd Length: 67  Bit Score: 56.48  E-value: 5.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110815813 1111 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPiIKFDLNKPVRVCNICF 1161
Cdd:cd15742    12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYP-LKYLKDRPAKVCDGCF 61
BTB_POZ_roadkill-like cd18345
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
61-166 6.76e-10

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster protein roadkill and similar proteins; Drosophila melanogaster protein roadkill, also called Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349654 [Multi-domain]  Cd Length: 121  Bit Score: 57.94  E-value: 6.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   61 LYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIYTDE---LEFREDD 132
Cdd:cd18345    12 LFERSAFSDVTLCVGGREFQAHKAILAARSPVFNAMFEHEMEErkqnrVEITDVDHEVMREMLRFIYTGKapnLDKMADD 91
                          90       100       110
                  ....*....|....*....|....*....|....
gi 110815813  133 vflteLMKLANRFQLQLLRERCEKGVMSLVNVRN 166
Cdd:cd18345    92 -----LLAAADKYALERLKVMCEEALCSNLSVEN 120
Ank_2 pfam12796
Ankyrin repeats (3 copies);
593-686 1.04e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 1.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   593 LGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHqadINVSRTQDGETALQLAIRNQLPLVV 672
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 110815813   673 DAICTRGADMSVPD 686
Cdd:pfam12796   78 KLLLEKGADINVKD 91
BTB_POZ_RCBTB1_2 cd18298
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
68-156 1.22e-09

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2; The RCC1-related guanine nucleotide exchange factor (GEF) family includes RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2, both of which are chromosome condensation regulator-like guanine nucleotide exchange factors. They contain an RCC1 repeat, a BTB domain, and a BACK domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349607 [Multi-domain]  Cd Length: 108  Bit Score: 56.88  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   68 SDLKIKVGDRHISAHKFVLAARSD--SWSLANLSSTKELD---LSDANPEVTMTMLRWIYTDELEFREDDVFltELMKLA 142
Cdd:cd18298    13 SDLKFRVDGKYIYVHKAILKIRCEyfRSMFQSHWNEDDKNvieIDQYSYPVYYAFLRYLYTDQVDLPPEDAI--GLLDLA 90
                          90
                  ....*....|....
gi 110815813  143 NRFQLQLLRERCEK 156
Cdd:cd18298    91 NSYCEERLKKLCED 104
BTB2_POZ_BTBD8 cd18286
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
61-152 1.35e-09

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 8 (BTBD8); BTBD8 is a BTB-domain-containing Kelch-like protein that may play a role in developmental processes. It may also act as a protein-protein adaptor in a transcription complex and thus be involved in brain development. BTBD8 contains two BTB domains. This model corresponds to the second domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349595 [Multi-domain]  Cd Length: 121  Bit Score: 56.88  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   61 LYEQEQYSDLKIKVGDRHISAHKFVLAARS--------DSWSlanLSSTKELDLSDANPEVTMTMLRWIYTDELEFrEDD 132
Cdd:cd18286    11 LFLNGEDSDITIKVDGKTFKAHRCILCARSsyfaamlsGSWA---ESNSSEITLTGVSHAAVSFVLLFIYGGVLDL-PDD 86
                          90       100
                  ....*....|....*....|
gi 110815813  133 VFLTELMKLANRFQLQLLRE 152
Cdd:cd18286    87 VNLGELLSLADMYGLDGLKD 106
PHA03100 PHA03100
ankyrin repeat protein; Provisional
493-715 1.49e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  493 TPLHTACRHGLANLTAELLQQGANPNLQTE-EALPLPKEAasltsladsvhlqtpLHMAIAYNHPDVVSVILEQKANaLH 571
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKnNSTPLHYLS---------------NIKYNLTDVKEIVKLLLEYGAN-VN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  572 ATNNLQIIPDFSLKDSRDQTVlglalwtgmhTIAAQLLGSGAAINDTMSDGQTLLHMAIQ--RQDSKSALFLLEHQADIN 649
Cdd:PHA03100  101 APDNNGITPLLYAISKKSNSY----------SIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDIN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  650 V---------------SRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCD 714
Cdd:PHA03100  171 AknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250

                  .
gi 110815813  715 A 715
Cdd:PHA03100  251 I 251
PHA03100 PHA03100
ankyrin repeat protein; Provisional
901-1079 2.23e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  901 RVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQ-----DLPTICSVLLENGVDFAAVDENGNN 975
Cdd:PHA03100   29 DYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGIT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  976 ALHLAVMHgRLNNIRV--LLTECTVDAEAFNLRGQSPLHILGQYGKE---------------NAAAIFDLFLECmpGYPL 1038
Cdd:PHA03100  109 PLLYAISK-KSNSYSIveYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdiNAKNRVNYLLSY--GVPI 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 110815813 1039 DKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGV 1079
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
BTB_POZ_KLHL40_KBTBD5 cd18340
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
60-168 2.73e-09

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 40 (KLHL40); KLHL40, also called Kelch repeat and BTB domain-containing protein 5 (KBTBD5) or sarcosynapsin, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. Mutations in KLHL40 may cause severe autosomal-recessive nemaline myopathy. KLHL40 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349649 [Multi-domain]  Cd Length: 134  Bit Score: 56.38  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   60 DLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW-----SLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 134
Cdd:cd18340    20 DLLDHNKFVDCVLKIKEKEFPCHRLVLAACSPYFramflSDLEESKKREIVLEDVDPDVMGKILHYIYTSEIEITEQNV- 98
                          90       100       110
                  ....*....|....*....|....*....|....
gi 110815813  135 lTELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18340    99 -QDIFAAANMFQIPSIFTVCVSFLQKRLCLSNCL 131
PHA02874 PHA02874
ankyrin repeat protein; Provisional
476-714 3.18e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 3.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  476 FLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLqteeaLPLPK-EAASLTSLADS--------VHLQTP 546
Cdd:PHA02874   53 LFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI-----LPIPCiEKDMIKTILDCgidvnikdAELKTF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  547 LHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLL 626
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGA-------------DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  627 HMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAI---RNQLPLVVDaictrGADMSVPDEKGNPPLWLALANNLE- 702
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHIMN-KCKNGFTPLHNAIihnRSAIELLIN-----NASINDQDIDGSTPLHHAINPPCDi 268
                         250
                  ....*....|..
gi 110815813  703 DIASTLVRHGCD 714
Cdd:PHA02874  269 DIIDILLYHKAD 280
FYVE_WDFY2 cd15757
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ...
1103-1160 3.44e-09

FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. WDFY2 contains WD40 motifs and a FYVE domain.


Pssm-ID: 277296 [Multi-domain]  Cd Length: 70  Bit Score: 54.30  E-value: 3.44e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110815813 1103 PPWCDGSYCYECTARF-----------GVTTRKHHCRHCGRLLCHKCSTKE--IPIIKFDLNkpVRVCNIC 1160
Cdd:cd15757     1 PEWLDSDSCQKCDQPFfwnfkqmwdskKIGLRQHHCRKCGKAVCGKCSSKRstIPLMGFEFE--VRVCDSC 69
BTB1_POZ_RhoBTB cd18299
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
60-155 3.47e-09

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing proteins (RhoBTB); RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. In vertebrates, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349608 [Multi-domain]  Cd Length: 103  Bit Score: 55.30  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   60 DLYEQEQYSDLKIKVGDRH-ISAHKFVLAARSDSWSLANLSSTK-ELDlSDANPEVTMTMLRWIYTDELEFREDDvfLTE 137
Cdd:cd18299     5 NLLHSPSCADVVFILQGGVrIFAHRIVLAAASSVFADLFLMMTVvTLD-SDITPEAFRRVLEFLYTGVLDENEDD--LKE 81
                          90
                  ....*....|....*...
gi 110815813  138 LMKLANRFQLQLLRERCE 155
Cdd:cd18299    82 LKDAAELLELFDLVMMCT 99
PHA03095 PHA03095
ankyrin-like protein; Provisional
480-831 3.75e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.42  E-value: 3.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  480 NGAHVNHRNKWGETPLHTACRHGLANLTAE---LLQQGANPNlqteealplpkeAASLTSLadsvhlqTPLHMAIAYNhp 556
Cdd:PHA03095   36 AGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVN------------APERCGF-------TPLHLYLYNA-- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  557 DVVSVIleqkanalhatnnlqiipDFslkdsrdqtvlglalwtgmhtiaaqLLGSGAAINDTMSDGQTLLH--MAIQRQD 634
Cdd:PHA03095   95 TTLDVI------------------KL-------------------------LIKAGADVNAKDKVGRTPLHvyLSGFNIN 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  635 SKSALFLLEHQADINvSRTQDGETALQLAIRNQ------LPLVVDAictrGADMSVPDEKGNPPLWlALANNL---EDIA 705
Cdd:PHA03095  132 PKVIRLLLRKGADVN-ALDLYGMTPLAVLLKSRnanvelLRLLIDA----GADVYAVDDRFRSLLH-HHLQSFkprARIV 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  706 STLVRHGCDATcwgpGPGGCLQTLLHRAidenNEPTAC------FLIRSGCDVNsprqpgangegeEEARDGQTPLHLAA 779
Cdd:PHA03095  206 RELIRAGCDPA----ATDMLGNTPLHSM----ATGSSCkrslvlPLLIAGISIN------------ARNRYGQTPLHYAA 265
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110815813  780 SWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQL-LVSHPDIHL 831
Cdd:PHA03095  266 VFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAaLAKNPSAET 318
BTB_POZ_SPOP-like cd18279
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
53-166 6.37e-09

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein (SPOP) and similar proteins; This family includes speckle-type POZ protein (SPOP), speckle-type POZ protein-like (SPOPL), TD and POZ domain-containing proteins (TDPOZ), Drosophila melanogaster protein roadkill and similar proteins. Both, SPOP and SPOPL, serve as adaptors of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that mediate the ubiquitination and proteasomal degradation of target proteins. TDPOZ is a family of bipartite animal and plant proteins that contain a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domains. TDPOZ proteins may be nuclear scaffold proteins probably involved in transcription regulation in early development and other cellular processes. Drosophila melanogaster protein roadkill, also called Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349588 [Multi-domain]  Cd Length: 120  Bit Score: 55.23  E-value: 6.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   53 RLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIYTDE-- 125
Cdd:cd18279     4 RLAEDLGNLWENSRFTDCCLCVGGQEFQAHKAILAARSPVFSAMFEHEMEEskknrVEINDVDPEVFKEMMRFIYTGKap 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 110815813  126 -LEFREDDvflteLMKLANRFQLQLLRERCEKGVMSLVNVRN 166
Cdd:cd18279    84 nLDKMADD-----LLAAADKYALERLKVMCEDALCSNLSVEN 120
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
1111-1161 7.92e-09

FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.


Pssm-ID: 277288 [Multi-domain]  Cd Length: 51  Bit Score: 52.51  E-value: 7.92e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110815813 1111 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlNKPVRVCNICF 1161
Cdd:cd15749     2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRKG-NQKQKVCKQCH 51
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
1111-1161 8.28e-09

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.


Pssm-ID: 277275 [Multi-domain]  Cd Length: 56  Bit Score: 52.57  E-value: 8.28e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110815813 1111 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPI---IKFDLN-KPVRVCNICF 1161
Cdd:cd15736     2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLnlsAYDPRNgKWYRCCHSCF 56
BTB_POZ_BTBD17 cd18292
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
47-156 9.04e-09

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 17 (BTBD17); BTBD17, also called galectin-3-binding protein-like, is a BTB domain-containing protein. Its function remains unclear. It may be associated with hepatocellular carcinoma. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349601 [Multi-domain]  Cd Length: 114  Bit Score: 54.60  E-value: 9.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   47 SESFISRLlaivADLYEQEQYSDLKIKVGDRHISAHKFVLAARSD--------SWSLANLSSTKELDLSDANPEVTMTML 118
Cdd:cd18292     1 SREFLQDI----AQLYNNEELSDIVLRVGGKVFHAHRLILAKSSDvfrvmlsnDWWSESKQSEIELVEDPECAAVFEKFL 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 110815813  119 RWIYTDELEFREDDVFltELMKLANRFQLQLLRERCEK 156
Cdd:cd18292    77 RYLYTGQISVNLETAL--PLLMLADKYNVTDLKQLCVD 112
PHA02874 PHA02874
ankyrin repeat protein; Provisional
481-697 1.16e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  481 GAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVS 560
Cdd:PHA02874  114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG-------------------CYPIHIAIKHNFFDIIK 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  561 VILEQKANAlhatnnlqiipdfSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRqdSKSALF 640
Cdd:PHA02874  175 LLLEKGAYA-------------NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH--NRSAIE 239
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  641 LLEHQADINVSRTqDGETALQLAIrnQLPL---VVDAICTRGADMSVPDEKGNPPLWLAL 697
Cdd:PHA02874  240 LLINNASINDQDI-DGSTPLHHAI--NPPCdidIIDILLYHKADISIKDNKGENPIDTAF 296
BTB_POZ_KLHL1-like cd18234
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
68-168 1.62e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins KLHL1, KLHL4 and KLHL5; This family contains the Kelch-like proteins: KLHL1, KLHL4 and KLHL5, all of which share high identity and similarity with the Drosophila kelch protein, a component of ring canals. KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels. Family members contain a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349543 [Multi-domain]  Cd Length: 105  Bit Score: 53.52  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   68 SDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTK-----ELDLSDANPEVTMTMLRWIYTDELEFREDDVflTELMKLA 142
Cdd:cd18234     2 CDVILIAGDRRIPAHRLVLSAVSDYFAAMFTNDVReateeEIKLKDVDPDALWTLVQYCYTGRLELKEDNV--ESLLATA 79
                          90       100
                  ....*....|....*....|....*.
gi 110815813  143 NRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18234    80 CLLQLSEVVEACCGFLMKQLHPSNCL 105
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
1113-1161 1.78e-08

FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277277 [Multi-domain]  Cd Length: 61  Bit Score: 51.94  E-value: 1.78e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 110815813 1113 ECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1161
Cdd:cd15738    13 SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGHLSQRPVPVCRACY 61
Ank_2 pfam12796
Ankyrin repeats (3 copies);
476-568 1.80e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.81  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   476 FLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQgANPNLQTEEalplpkeaasltsladsvhlQTPLHMAIAYNH 555
Cdd:pfam12796   15 LLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG--------------------RTALHYAARSGH 73
                           90
                   ....*....|...
gi 110815813   556 PDVVSVILEQKAN 568
Cdd:pfam12796   74 LEIVKLLLEKGAD 86
Ank_4 pfam13637
Ankyrin repeats (many copies);
773-824 2.33e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 2.33e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 110815813   773 TPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLV 824
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
660-754 3.20e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 3.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   660 LQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHgCDATCWGPGpggclQTLLHRAIDENNE 739
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-----RTALHYAARSGHL 74
                           90
                   ....*....|....*
gi 110815813   740 PTACFLIRSGCDVNS 754
Cdd:pfam12796   75 EIVKLLLEKGADINV 89
BTB_POZ_BPM_plant cd18280
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
59-155 3.50e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in plant BTB/POZ-MATH (BPM) protein family; The BPM protein family includes Arabidopsis thaliana BTB/POZ and MATH domain-containing proteins, AtBPM1-6, and similar proteins from other plants. BPM protein, also called protein BTB-POZ and MATH domain, may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349589 [Multi-domain]  Cd Length: 121  Bit Score: 53.10  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   59 ADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW------SLANlSSTKELDLSDANPEVTMTMLRWIYTDEL------ 126
Cdd:cd18280     6 GALLESEEGADVTFNVDGEKFRAHKLVLAARSPVFrsmlfgPMRE-ENEGEIVIEDVEPPVFKALLHFIYKDELpddvep 84
                          90       100       110
                  ....*....|....*....|....*....|...
gi 110815813  127 ----EFREDDVFLTELMKLANRFQLQLLRERCE 155
Cdd:cd18280    85 agsdSSSLDTTMAQHLLAAADRYALERLRLLCE 117
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
771-898 3.60e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 3.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  771 GQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLL-----VSHPDIHLNVrdrqgltpfACA 845
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasISDPHAAGDL---------LCT 628
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110815813  846 MTFKNNKSAEAILKRESGAAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANV 898
Cdd:PLN03192  629 AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02878 PHA02878
ankyrin repeat protein; Provisional
271-421 4.20e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 4.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  271 IATTLVSHKADVDMVDK-SGWSLLHKGIQRGDLFAATFLIKNGAFVNAATLGaQETPLHLVALYSSKKhsadvmsemaqI 349
Cdd:PHA02878  149 ITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKT-NNSPLHHAVKHYNKP-----------I 216
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110815813  350 AEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLDLELKdhegSTALWLAVQHITVSSDQSVN 421
Cdd:PHA02878  217 VHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAK----SYILGLTALHSSIKSERKLK 284
BTB_POZ_KLHL8 cd18238
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
60-168 4.26e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 8 (KLHL8); KLHL8 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for the ubiquitination and degradation of rapsyn, a postsynaptic protein required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349547 [Multi-domain]  Cd Length: 120  Bit Score: 52.68  E-value: 4.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   60 DLYEQEQYSDLKIKVGDRHISAHKFVLAARSD---SWSLANLSSTKE--LDLSDANPEVTMTMLRWIYTDELEFREDDVf 134
Cdd:cd18238     8 QFYENGELCDVTLKVGEKSIHCHRLVLACVSPyfrAMFTSEMAESKQdsITIKDIDEEAVELLVDFAYTGKLTLTVDNV- 86
                          90       100       110
                  ....*....|....*....|....*....|....
gi 110815813  135 lTELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18238    87 -QSLLYAASLLQVEEVAKACCEFMKDHLHPSNCL 119
Ank_2 pfam12796
Ankyrin repeats (3 copies);
342-411 4.46e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 4.46e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   342 VMSEMAQIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLDLelkDHEGSTALWLAVQH 411
Cdd:pfam12796    5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARS 71
BTB_POZ_KBTBD3_BKLHD3 cd18271
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
47-169 5.34e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 3 (KBTBD3); KBTBD3, also called BTB and kelch domain-containing protein 3 (BKLHD3), contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349580 [Multi-domain]  Cd Length: 130  Bit Score: 52.91  E-value: 5.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   47 SESFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELD-----LSDANPEVTMTMLRWI 121
Cdd:cd18271     4 AECHGQQILSVLQNFREQNAFFDFNIIVKDETIPCHRCVLAACSDFFRAMFEVNMKERDdgsvtISNLSPKAVKAFLDYA 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 110815813  122 YTDELEFREDDVFLteLMKLANRFQLQLLRERCEKGVMSLVNVRNCIR 169
Cdd:cd18271    84 YTGKAEITDDNVEM--FFQMSSFLQVSLLSKACSDFLIKSIDLTNCLQ 129
BTB_POZ_KLHL40-like cd18269
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
60-147 5.86e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins, KLHL40 and KLHL41; This family includes Kelch-like proteins, KLHL40 and KLHL41. KLHL40 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. KLHL41 is a novel kelch related protein that is involved in pseudopod elongation in transformed cells. They both contain a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349578 [Multi-domain]  Cd Length: 133  Bit Score: 52.79  E-value: 5.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   60 DLYEQEQYSDLKIKVGDRHISAHKFVLAA-----RSDSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 134
Cdd:cd18269    20 DLLDENKFVDCVLKIGDKEFPCHRLVLAAcspyfRAMFLSDLEESKKKEVVLEDVDPDVMGMILKYLYTSEIDLNDQNV- 98
                          90
                  ....*....|...
gi 110815813  135 lTELMKLANRFQL 147
Cdd:cd18269    99 -QDIFALASRFQI 110
BTB_POZ_KLHL27_IPP cd18256
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
52-168 5.98e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in intracisternal A particle-promoted polypeptide (IPP); IPP, also called Kelch-like protein 27 (KLHL27) or actin-binding protein IPP, is an actin-binding protein that may play a role in organizing the actin cytoskeleton. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349565 [Multi-domain]  Cd Length: 125  Bit Score: 52.41  E-value: 5.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   52 SRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSL-----ANLSSTKELDLSDANPEVTMTMLRWIYTDEL 126
Cdd:cd18256     5 SLILAQLNKLRGQHEFCDVQLQVGMELFSVHRLVLAASSPYFAAlfaggMSESSKDVVQIHGVEPDIFHILLDFIYTGVV 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 110815813  127 EFREDDVflTELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18256    85 EVTVSNV--QELLVAADMLQLTEVVEICCEFLKGQLHPSNCI 124
Ank_2 pfam12796
Ankyrin repeats (3 copies);
730-801 7.78e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 7.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   730 LHRAIDENNEPTACFLIRSGCDVNSPRQPG-------ANGEGEEEAR------------DGQTPLHLAASWGLEETVQCL 790
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGrtalhlaAKNGHLEIVKlllehadvnlkdNGRTALHYAARSGHLEIVKLL 80
                           90
                   ....*....|.
gi 110815813   791 LEFGANVNAQD 801
Cdd:pfam12796   81 LEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
308-716 9.29e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.19  E-value: 9.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  308 LIKNGAFVN-AATLGaqETPLHLVALYSSKKhsadvmseMAQIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQL 386
Cdd:PHA03095   33 LLAAGADVNfRGEYG--KTPLHLYLHYSSEK--------VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  387 LQCKQLDLELKDHEGSTALwlavqHITVSsdqsvNPFEDVPVVNgtsfdensfaarliqrgshtdapdtatgncllqraa 466
Cdd:PHA03095  103 LIKAGADVNAKDKVGRTPL-----HVYLS-----GFNINPKVIR------------------------------------ 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  467 gagneaaalFLATNGAHVNHRNKWGETPLHTACRHglANLTAELLqqganpNLqteealpLPKEAASLTslADSVHLQTP 546
Cdd:PHA03095  137 ---------LLLRKGADVNALDLYGMTPLAVLLKS--RNANVELL------RL-------LIDAGADVY--AVDDRFRSL 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  547 LHMAIAYNHPD--VVSVILEQKANALhATNNLQIIPDFSLKdsrdqtvlglALWTGMHTIAAQLLGSGAAINDTMSDGQT 624
Cdd:PHA03095  191 LHHHLQSFKPRarIVRELIRAGCDPA-ATDMLGNTPLHSMA----------TGSSCKRSLVLPLLIAGISINARNRYGQT 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  625 LLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAIRNQlplvvDAICTRGAdmsvpdEKGNPPLwLALANNLEDI 704
Cdd:PHA03095  260 PLHYAAVFNNPRACRRLIALGADINA-VSSDGNTPLSLMVRNN-----NGRAVRAA------LAKNPSA-ETVAATLNTA 326
                         410
                  ....*....|..
gi 110815813  705 ASTLVRHGCDAT 716
Cdd:PHA03095  327 SVAGGDIPSDAT 338
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
1107-1161 9.39e-08

FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.


Pssm-ID: 277265 [Multi-domain]  Cd Length: 58  Bit Score: 49.87  E-value: 9.39e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110815813 1107 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCStkEIPIIKFDLNKPVRVCNICF 1161
Cdd:cd15726     6 DVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACS--NFYVLTAHGGKKERCCKACF 58
PHA02874 PHA02874
ankyrin repeat protein; Provisional
297-630 9.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 9.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  297 IQRGDLFAATFLIKNGAFVN------------AATLGAQETPLHLV--ALYSSKKHSADVMSEMAQiaeALLQAGANPNM 362
Cdd:PHA02874   43 IRSGDAKIVELFIKHGADINhintkiphplltAIKIGAHDIIKLLIdnGVDTSILPIPCIEKDMIK---TILDCGIDVNI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  363 QDSKGRTPLHVSIMAGNEYVFSQLLQCKQlDLELKDHEGSTALWLAVQHitvssdqsvNPFEDVPVvngtsfdensfaar 442
Cdd:PHA02874  120 KDAELKTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKH---------NFFDIIKL-------------- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  443 LIQRGSHTDAPDTaTGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRHGLAnlTAELLQQGANPNLQte 522
Cdd:PHA02874  176 LLEKGAYANVKDN-NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS--AIELLINNASINDQ-- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  523 ealplpkeaasltsladSVHLQTPLHMAIayNHP---DVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLGLAL-W 598
Cdd:PHA02874  251 -----------------DIDGSTPLHHAI--NPPcdiDIIDILLYHKA-------------DISIKDNKGENPIDTAFkY 298
                         330       340       350
                  ....*....|....*....|....*....|....
gi 110815813  599 TGMHTIAAQLLGSGAAIN--DTMSDGQTLLHMAI 630
Cdd:PHA02874  299 INKDPVIKDIIANAVLIKeaDKLKDSDFLEHIEI 332
PHA02876 PHA02876
ankyrin repeat protein; Provisional
292-672 1.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 1.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  292 LLHKGIQRGDLFAATFLIKNGAFVNAATLGAQeTPLHLVALYSSkkhsadvmsemAQIAEALLQAGANPNMQDSKGRTPL 371
Cdd:PHA02876  148 LIKERIQQDELLIAEMLLEGGADVNAKDIYCI-TPIHYAAERGN-----------AKMVNLLLSYGADVNIIALDDLSVL 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  372 HVSIMAGN----EYVFSQLLQCKQLDLEL----KDHEGSTALWLAVQHITVSsdqSVNPFEDVPVVNGTSFDENS-FAAR 442
Cdd:PHA02876  216 ECAVDSKNidtiKAIIDNRSNINKNDLSLlkaiRNEDLETSLLLYDAGFSVN---SIDDCKNTPLHHASQAPSLSrLVPK 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  443 LIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACR-HGLANLTAELLQQGANPNlqt 521
Cdd:PHA02876  293 LLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVN--- 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  522 eealplpkeaasltslADSVHLQTPLHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLGLALW-TG 600
Cdd:PHA02876  370 ----------------ARDYCDKTPIHYAAVRNNVVIINTLLDYGA-------------DIEALSQKIGTALHFALCgTN 420
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815813  601 MHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSAL-FLLEHQADINVsrtqdgetalqLAIRNQLPLVV 672
Cdd:PHA02876  421 PYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIeMLLDNGADVNA-----------INIQNQYPLLI 482
PHA02875 PHA02875
ankyrin repeat protein; Provisional
254-409 1.67e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  254 HNGDLALDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNAATLGAQETPLHLvaly 333
Cdd:PHA02875   33 YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHL---- 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110815813  334 SSKKHSADVMsemaqiaEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLdLELKDHEGSTALWLAV 409
Cdd:PHA02875  109 ATILKKLDIM-------KLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAM 176
BTB_POZ_KBTBD4 cd18272
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
52-169 2.01e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 4 (KBTBD4); KBTBD4, also called BTB and kelch domain-containing protein 4 (BKLHD4), is a BTB-BACK-Kelch domain protein belonging to a large family of cullin-RING ubiquitin ligase adaptors that facilitate the ubiquitination of target substrates. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349581 [Multi-domain]  Cd Length: 140  Bit Score: 51.43  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   52 SRLLAIVADL-YEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIYTDE 125
Cdd:cd18272    16 SRVAQSIMDLcLEDGLFADVTISVEGKEFQLHRLVLSAQSCFFRSMFTSNLKEarnrvIELKDVSESVFQLLVDYIYHGT 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 110815813  126 LEFREDDvfLTELMKLANRFQLQLLRERCEKGVMSLVNVRNCIR 169
Cdd:cd18272    96 VKLRVEE--LQETYEVADMYQLTALFEECSRFLARTVQVRNCLQ 137
PHA02875 PHA02875
ankyrin repeat protein; Provisional
876-1069 2.15e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  876 LHVAVQNSDIESVLFLISVHANVNSRVQDASklTPLHLAVQAGSEIIVRNLLLAGAKVNELT-KHRQTALHLAAQQDLPT 954
Cdd:PHA02875   39 IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE--SELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  955 ICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtectvdaeafnlrgqsplhilgqygKENAAaifdlflecmp 1034
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI-------------------------DHKAC----------- 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 110815813 1035 gypLDKPDADGSTVLLLAYMKGNANLCRAIVRSGA 1069
Cdd:PHA02875  161 ---LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
PHA02878 PHA02878
ankyrin repeat protein; Provisional
726-928 2.44e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  726 LQTLLHRAIDENNEPTACFLIRSGCDVNSPRqpgangegeeeaRDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGR 805
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANVNIPD------------KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  806 TPIHVAISSQHGV-IIQLLVSHpDIHLNVRDR-QGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHVAVQNS 883
Cdd:PHA02878  236 TPLHISVGYCKDYdILKLLLEH-GVDVNAKSYiLGLTA----------------------------------LHSSIKSE 280
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110815813  884 DIESVLflISVHANVNSrvQDASKLTPLHLAVQAGSEIIVRNLLL 928
Cdd:PHA02878  281 RKLKLL--LEYGADINS--LNSYKLTPLSSAVKQYLCINIGRILI 321
PHA03098 PHA03098
kelch-like protein; Provisional
72-239 2.64e-07

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 54.77  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   72 IKVGDRHISAHKFVLAARSDSWS--LANLSSTKELDLSDaNPEVTMTMLRWIYTDELEFREDDVflTELMKLANRFQLQL 149
Cdd:PHA03098   16 IVNGGGIIKVHKIILSSSSEYFKkmFKNNFKENEINLNI-DYDSFNEVIKYIYTGKINITSNNV--KDILSIANYLIIDF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  150 LRERCEKGVMSLVNVRNCIRFYQTAEELNASTLMNYCAEIIASHWDDLRK-EDFSSMSAQLLYKMIKSKTeyplhkaIKV 228
Cdd:PHA03098   93 LINLCINYIIKIIDDNNCIDIYRFSFFYGCKKLYSAAYNYIRNNIELIYNdPDFIYLSKNELIKILSDDK-------LNV 165
                         170
                  ....*....|.
gi 110815813  229 EREDVVFLYLI 239
Cdd:PHA03098  166 SSEDVVLEIII 176
BTB_POZ_BTBD1 cd18346
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
40-154 3.50e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 1 (BTBD1); BTBD1, also called Hepatitis C virus NS5A-transactivated protein 8 or HCV NS5A-transactivated protein 8, is a BTB-domain-containing Kelch-like protein that is expressed in skeletal muscle and interacts with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. BTBD1 may serve as substrate-specific adaptor of an E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349655 [Multi-domain]  Cd Length: 133  Bit Score: 50.44  E-value: 3.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   40 QANKESSSESFisrllaivADLYEQEQYSDLKIKVGD----------RHISAHKFVLAARS---DSWSLANLSSTK-ELD 105
Cdd:cd18346     3 QATKSSLKERF--------AFLFNNELLSDVRFVVGKgrprgpgpgaQRIPAHRFVLAAGSavfDAMFNGGMATTSaEIE 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 110815813  106 LSDANPEVTMTMLRWIYTDELEFREDDVFLTelMKLANRFQLQLLRERC 154
Cdd:cd18346    75 LPDVEPAAFLALLRFLYSDEVQIGPETVMTT--LYTAKKYAVPALEAHC 121
PHA03100 PHA03100
ankyrin repeat protein; Provisional
477-650 3.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  477 LATNGAHVNHRNKWGETPLHTACRHGLANLT--AELLQQGANPNLQTEEALPLpkeaasltsladsvhlqtpLHMAIAYN 554
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKKSNSYSivEYLLDNGANVNIKNSDGENL-------------------LHLYLESN 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  555 HPD--VVSVILEQKANaLHATNNLQII----PDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHM 628
Cdd:PHA03100  153 KIDlkILKLLIDKGVD-INAKNRVNYLlsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
                         170       180
                  ....*....|....*....|..
gi 110815813  629 AIQRQDSKSALFLLEHQADINV 650
Cdd:PHA03100  232 AILNNNKEIFKLLLNNGPSIKT 253
BTB_POZ_KLHL41_KBTBD10 cd18341
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
60-168 5.11e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 41 (KLHL41); KLHL41 is also called Kel-like protein 23, Kelch repeat and BTB domain-containing protein 10 (KBTBD10), Kelch-related protein 1 (Krp1), or sarcosine. It is a novel kelch-related protein that is involved in pseudopod elongation in transformed cells. It is also involved in skeletal muscle development and differentiation. It regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349650 [Multi-domain]  Cd Length: 133  Bit Score: 49.84  E-value: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   60 DLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSS-----TKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 134
Cdd:cd18341    20 ELLDENKFVDCTLKAGDKSLPCHRLILAACSPYFREYFLSEeseekKKEVVLDNVDPNIMDMILKYLYSAEIDLNDGNV- 98
                          90       100       110
                  ....*....|....*....|....*....|....
gi 110815813  135 lTELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18341    99 -QDIFALASRFQIPSVFTVCVTYLQKRLSPANCL 131
PHA02878 PHA02878
ankyrin repeat protein; Provisional
349-632 5.94e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 5.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  349 IAEALLQAGANPNMQDSKGRTPLHVSIMAGN----EYVFSQLLQCKQLDLELKDHEGSTALWLAVQHITVSSDQSVNPFE 424
Cdd:PHA02878   52 VVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTI 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  425 DVPVVNGTSFD---ENSFAARLIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRH 501
Cdd:PHA02878  132 DLVYIDKKSKDdiiEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  502 GLANLTAELLQQGANPNlqteealplpkeaasltslADSVHLQTPLHMAIAY-NHPDVVSVILEQKA--NALHATNNLQI 578
Cdd:PHA02878  212 YNKPIVHILLENGASTD-------------------ARDKCGNTPLHISVGYcKDYDILKLLLEHGVdvNAKSYILGLTA 272
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 110815813  579 IpDFSLKDSRdqtVLGLalwtgmhtiaaqLLGSGAAINDTMSDGQTLLHMAIQR 632
Cdd:PHA02878  273 L-HSSIKSER---KLKL------------LLEYGADINSLNSYKLTPLSSAVKQ 310
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
563-711 6.12e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  563 LEQKANALHATNNLQIIPDFSL--KDSRDQTVLglalwtgmHTIAA---QLLGSGaaindtmsdgqtllhmaiqrqDSKS 637
Cdd:PTZ00322   47 IDTHLEALEATENKDATPDHNLttEEVIDPVVA--------HMLTVelcQLAASG---------------------DAVG 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110815813  638 ALFLLEHQADINvSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRH 711
Cdd:PTZ00322   98 ARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
347-488 9.10e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 9.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  347 AQIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLELKDHEGSTALW--LAVQH-----ITVSSDQS 419
Cdd:PLN03192  538 AALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLK-HACNVHIRDANGNTALWnaISAKHhkifrILYHFASI 616
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110815813  420 VNPFedvpvvngTSFDENSFAAR---------LIQRGSHTDAPDTaTGNCLLQRAAGAGNEAAALFLATNGAHVNHRN 488
Cdd:PLN03192  617 SDPH--------AAGDLLCTAAKrndltamkeLLKQGLNVDSEDH-QGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_2 pfam12796
Ankyrin repeats (3 copies);
260-364 1.18e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   260 LDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLIKNgAFVNAATLGaqETPLHLVALYSSKKhs 339
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG--RTALHYAARSGHLE-- 75
                           90       100
                   ....*....|....*....|....*
gi 110815813   340 advmsemaqIAEALLQAGANPNMQD 364
Cdd:pfam12796   76 ---------IVKLLLEKGADINVKD 91
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
1111-1161 1.30e-06

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277279 [Multi-domain]  Cd Length: 54  Bit Score: 46.53  E-value: 1.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 110815813 1111 CYECTARFG-VTTRKHHCRHCGRLLCHKCSTkeipiIKFDLNKPVRVCNICF 1161
Cdd:cd15740     8 CKGCNESFNsITKRRHHCKQCGAVICGKCSE-----FKDLASRHNRVCRDCF 54
BTB_POZ_NS1BP cd18306
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
50-168 1.32e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Influenza virus NS1A-binding protein (NS1-BP); NS1-BP is also called NS1-binding protein, aryl hydrocarbon receptor-associated protein 3 (ARA3), or IVNS1ABP. It is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through its kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. NS1-BP contains BTB and BACK domains at the N-terminal region and kelch repeats at the C-terminal region. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349615 [Multi-domain]  Cd Length: 124  Bit Score: 48.41  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   50 FISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSdSWSLANLSSTKE------LDLSDANPEVTMTMLRWIYT 123
Cdd:cd18306     1 HPESVLAKLNALRKNRQFCDVILQVGGHEIPAHRAVLACAS-PYLFELFSSDSDgesiltVKLDGLDPDAVEVLVNYAYT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 110815813  124 DELEFREDDVFltELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18306    80 SRLEVPADLVK--SVYSAAKKLKMDRVKKACGDFLLEKLTPQNCI 122
BTB_POZ_ABTB2-like cd18297
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
56-155 1.85e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) and similar proteins; This family includes ABTB2, BTBD11, plant ARM repeat protein interacting with ABF2 (ARIA), and similar proteins. ABTB2, also called bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation, and prevent translation. The BTBD11 gene has been recently identified as an all-trans retinoic acid (atRA)-responsive gene that lies downstream of atRA and its receptors in the regulation of neurite outgrowth and cell adhesion in neural as well as non-neural tissues. ARIA is an armadillo (ARM) repeat and BTB domain-containing protein that acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349606 [Multi-domain]  Cd Length: 117  Bit Score: 48.04  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   56 AIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW-SLANL----SSTKELDLSDANPEVTMTMLRWIYT---DELE 127
Cdd:cd18297     1 RIDPHYVNNPEMSDVTFLVEGRPFYAHKIVLVTASDRFkSMLSSgsteAQTPVIEIPDIRYDIFQLMMQYLYTggvESLD 80
                          90       100
                  ....*....|....*....|....*...
gi 110815813  128 FREDDVFltELMKLANRFQLQLLRERCE 155
Cdd:cd18297    81 VAQDDAL--ELLRAASFFQLDGLKRHCE 106
BTB_POZ_KLHL18 cd18247
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
49-154 2.31e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 18 (KLHL18); KLHL18 acts as a substrate-specific adaptor for a Cullin3 E3 ubiquitin-protein ligase complex that regulates mitotic entry and ubiquitylates Aurora-A. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349556 [Multi-domain]  Cd Length: 116  Bit Score: 47.66  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   49 SFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW------SLANlSSTKELDLSDANPEVTMTMLRWIY 122
Cdd:cd18247     1 DLPSSGFPVMEEIRRQGKLCDVTLKVGDQKFSAHRIVLAATIPYFhamfthDMVE-SKQDEITMQGIEPSALEALINFAY 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 110815813  123 TDELEFREDDVflTELMKLANRFQLQLLRERC 154
Cdd:cd18247    80 SGRIAIDTSNV--QSLLVGASFLQLQSVKDAC 109
PHA02874 PHA02874
ankyrin repeat protein; Provisional
879-1018 2.48e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  879 AVQNSDIESVLFLISVHANVNSrvQDASKLTPLHLAVQAGSEIIVRNLLL-----------------------AGAKVNE 935
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINH--INTKIPHPLLTAIKIGAHDIIKLLIDngvdtsilpipciekdmiktildCGIDVNI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  936 LTKHRQTALHLAAQQ-DLPTIcSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPLHIL 1014
Cdd:PHA02874  120 KDAELKTFLHYAIKKgDLESI-KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EKGAYANVKDNNGESPLHNA 197

                  ....
gi 110815813 1015 GQYG 1018
Cdd:PHA02874  198 AEYG 201
Ank_4 pfam13637
Ankyrin repeats (many copies);
942-993 2.62e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.62e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 110815813   942 TALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLL 993
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
912-1002 2.63e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  912 HLAVqAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRV 991
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                          90
                  ....*....|.
gi 110815813  992 LLTECTVDAEA 1002
Cdd:PTZ00322  167 LSRHSQCHFEL 177
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
1111-1164 2.85e-06

FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.


Pssm-ID: 277262 [Multi-domain]  Cd Length: 62  Bit Score: 45.57  E-value: 2.85e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110815813 1111 CYECTARFGV-TTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKP------VRVCNICFDVL 1164
Cdd:cd15723     2 CTGCGASFSVlLKKRRSCNNCGNAFCSRCCSKKVPRSVMGATAPaaqretVFVCSGCNDKL 62
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
1124-1161 3.69e-06

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 45.10  E-value: 3.69e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 110815813 1124 KHHCRHCGRLLCHKCSTKEIPIIKFDLNkPVRVCNICF 1161
Cdd:cd15744    16 KHNCYNCGGTFCDACSSNELPLPSSIYE-PARVCDVCY 52
BTB_POZ_KLHL1 cd18335
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
63-168 3.84e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 1 (KLHL1); KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels. It may play a role in organizing the actin cytoskeleton the brain cells. KLHL1 contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349644 [Multi-domain]  Cd Length: 126  Bit Score: 47.35  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   63 EQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSST-----KELDLSDANPEVTMTMLRWIYTDELEFREDDVflTE 137
Cdd:cd18335    15 KQQQLCDVILIAGNRKIPAHRLVLSAVSDYFAAMFTSDVceakqEEIKMEGIDPNALWDLVQFAYTGCLELKEDTI--EN 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 110815813  138 LMKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18335    93 LLAAACLLQLSQVVEVCCHFLMKLLHPSNCL 123
PHA02946 PHA02946
ankyin-like protein; Provisional
782-1014 4.14e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 50.82  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  782 GLEET-VQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHpdihlnvrdrqGLTPFACAmtfKNNKSAEAILkr 860
Cdd:PHA02946   49 GLDERfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTH-----------GADPNACD---KQHKTPLYYL-- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  861 eSGAAEQVdnkgrnflhvavqnsdIESVLFLISVHANVNSRVqDASKLTPLhLAVQAGSEIIVRNLLLAGAKVNELTKHR 940
Cdd:PHA02946  113 -SGTDDEV----------------IERINLLVQYGAKINNSV-DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFG 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813  941 QTALHLAAQQDLPTICSV--LLENGVDFAAVDENGNNALHLaVMHGRLNNIRVL-LTECTVDAEAFNLRGQSPLHIL 1014
Cdd:PHA02946  174 KNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHI-VCSKTVKNVDIInLLLPSTDVNKQNKFGDSPLTLL 249
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
727-916 4.17e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 51.03  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  727 QTLLHRAIDENNEPTACFLIRSGCDVnsprQPGANGEGEEEARD-----GQTPLHLAASWGLEETVQCLLEFG---ANVN 798
Cdd:cd21882    74 QTALHIAIENRNLNLVRLLVENGADV----SARATGRFFRKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALE 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  799 AQDAEGRTPIHV--------------AISSQHGVIIQLLVSHPDIHLN-VRDRQGLTPFACAMTFKNNKSAEAILKRESG 863
Cdd:cd21882   150 AQDSLGNTVLHAlvlqadntpensafVCQMYNLLLSYGAHLDPTQQLEeIPNHQGLTPLKLAAVEGKIVMFQHILQREFS 229
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110815813  864 AAEQvdNKGRNF-------LHVA------VQNSDIESVLFLISVHANVNSRvQDASKLTPLHLAVQ 916
Cdd:cd21882   230 GPYQ--PLSRKFtewtygpVTSSlydlseIDSWEKNSVLELIAFSKKREAR-HQMLVQEPLNELLQ 292
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
770-801 4.67e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 4.67e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 110815813   770 DGQTPLHLAA-SWGLEETVQCLLEFGANVNAQD 801
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
BTB_POZ_BTBD3_6 cd18282
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
61-136 5.62e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD3 and BTBD6; This family includes BTB/POZ domain-containing proteins BTBD3 and BTBD6, both of which are BTB-domain-containing Kelch-like proteins. BTBD3 controls dendrite orientation toward active axons in mammalian neocortex. BTBD6 is required for proper embryogenesis and plays an essential evolutionary conserved role during neuronal development. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349591 [Multi-domain]  Cd Length: 108  Bit Score: 46.23  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   61 LYEQEQYSDLKIKVGD----RHISAHKFVLAARSDSW------SLANlsSTKELDLSDANPEVTMTMLRWIYTDELEFRE 130
Cdd:cd18282     1 MFNNELMADVHFIVGPpggtQRIPAHKYVLATGSSVFyamfygGLAE--NKNEIEIPDVEPAAFLNLLRYLYCDEIDLEP 78

                  ....*.
gi 110815813  131 DDVFLT 136
Cdd:cd18282    79 DTVLAT 84
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
476-682 6.01e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.64  E-value: 6.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  476 FLATNGAHvnHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNH 555
Cdd:PLN03192  512 LLGDNGGE--HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKG-------------------RTPLHIAASKGY 570
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  556 PDVVSVILEqkanalHATNnlqiipdFSLKDSRDQTVLGLALWTGMHTIaAQLLGSGAAINDTMSDGQtLLHMAIQRQDS 635
Cdd:PLN03192  571 EDCVLVLLK------HACN-------VHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHAAGD-LLCTAAKRNDL 635
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 110815813  636 KSALFLLEHQADINvSRTQDGETALQLAIRNQLPLVVDAICTRGADM 682
Cdd:PLN03192  636 TAMKELLKQGLNVD-SEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
727-916 6.15e-06

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 50.56  E-value: 6.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  727 QTLLHRAIDENNEPTACFLIRSGCDVNSPR-----QPGANGEGeeeARDGQTPLHLAASWGLEETVQCLLEFG---ANVN 798
Cdd:cd22193    77 QTALHIAIERRQGDIVALLVENGADVHAHAkgrffQPKYQGEG---FYFGELPLSLAACTNQPDIVQYLLENEhqpADIE 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  799 AQDAEGRTPIH--VAIS-----------SQHGVIIQLLVS-HPDIHLN-VRDRQGLTPFACAMTFKNNKSAEAILKRE-- 861
Cdd:cd22193   154 AQDSRGNTVLHalVTVAdntkentkfvtRMYDMILIRGAKlCPTVELEeIRNNDGLTPLQLAAKMGKIEILKYILQREik 233
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813  862 SGAAEQVDNKGRNFLHVAVQNS--DI--------ESVLFLISVHANVNSRvQDASKLTPLHLAVQ 916
Cdd:cd22193   234 EPELRHLSRKFTDWAYGPVSSSlyDLsnvdtcekNSVLEIIVYNSKIDNR-HEMLTLEPLNTLLQ 297
BTB_POZ_SPOP cd18342
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
53-166 7.17e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein (SPOP); SPOP, also called HIB homolog 1 or Roadkill homolog 1, is a novel nuclear speckle-type protein which serves as an adaptor of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and proteasomal degradation of target proteins, such as BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349651 [Multi-domain]  Cd Length: 125  Bit Score: 46.63  E-value: 7.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   53 RLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSL-----ANLSSTKELDLSDANPEVTMTMLRWIYTDELE 127
Cdd:cd18342     8 RLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAmfeheMEESKKNRVEINDVEPEVFKEMMCFIYTGKAP 87
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 110815813  128 frEDDVFLTELMKLANRFQLQLLRERCEKGVMSLVNVRN 166
Cdd:cd18342    88 --NLDKMADDLLAAADKYALERLKVMCEDALCSNLSVEN 124
BTB1_POZ_IBtk cd18301
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
69-124 7.57e-06

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in inhibitor of Bruton tyrosine kinase (IBtk); IBtk is an inhibitor or negative regulator of Bruton tyrosine kinase (Btk), which is required for B-cell differentiation and development. IBtk binds to the PH domain of Btk and down-regulates the Btk kinase activity. It contains two BTB domains. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349610 [Multi-domain]  Cd Length: 99  Bit Score: 45.74  E-value: 7.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813   69 DLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELDLSDANPEVTMT---------MLRWIYTD 124
Cdd:cd18301    20 DVVFQVGGKTFPAHKFILASRSDYFRKLFLSSLLTSEDAVGCDVVHIEkvppeifeqLLQFIYTD 84
BTB_POZ_KLHL4 cd18336
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
63-168 9.78e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 4 (KLHL4); KLHL4 shares high identity and similarity with the Drosophila kelch protein, a component of ring canals. It may be associated with X-linked cleft palate (CPX) and is also a candidate gene in the impairment of mullerian duct development. In addition, it has been identified as a target of insulin-like growth factor binding protein 5 (IGFBP5). KLHL4 contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349645 [Multi-domain]  Cd Length: 126  Bit Score: 46.19  E-value: 9.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   63 EQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIYTDELEFREDDVflTE 137
Cdd:cd18336    15 QHKQLCDVLLIAGNLKIPAHRLVLSAVSDYFAAMFTNDVREakqeeIKMEGVDPDALKALVHYAYTGVLELKEDTI--ES 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 110815813  138 LMKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18336    93 LLAAACLLQLSQVIDVCCNFLMKQLHPSNCL 123
PHA02876 PHA02876
ankyrin repeat protein; Provisional
257-567 1.02e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  257 DLALDLALSRrlESIATTLVSHKA--DVDMVDKSGWSLLHKGIQRGDLFA-ATFLIKNGAFVNAATLGAqETPLHLVA-- 331
Cdd:PHA02876  241 DLSLLKAIRN--EDLETSLLLYDAgfSVNSIDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKG-ETPLYLMAkn 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  332 ----------------------LYSSKKHSADVMSEMAQIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQC 389
Cdd:PHA02876  318 gydtenirtlimlgadvnaadrLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  390 KQlDLELKDHEGSTALWLAVqhitvssdQSVNPFEDVPVvngtsfdensfaarLIQRgshtdapdtatgncllqraagag 469
Cdd:PHA02876  398 GA-DIEALSQKIGTALHFAL--------CGTNPYMSVKT--------------LIDR----------------------- 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  470 neaaalflatnGAHVNHRNKWGETPLHTACRHGLA-NLTAELLQQGANPNlqteealplpkeaasltslADSVHLQTPLH 548
Cdd:PHA02876  432 -----------GANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVN-------------------AINIQNQYPLL 481
                         330
                  ....*....|....*....
gi 110815813  549 MAIAYNhpDVVSVILEQKA 567
Cdd:PHA02876  482 IALEYH--GIVNILLHYGA 498
Ank_2 pfam12796
Ankyrin repeats (3 copies);
293-398 1.07e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   293 LHKGIQRGDLFAATFLIKNGAFVNAaTLGAQETPLHLVALYSSkkhsadvmsemAQIAEALLQaGANPNMQDsKGRTPLH 372
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGH-----------LEIVKLLLE-HADVNLKD-NGRTALH 66
                           90       100
                   ....*....|....*....|....*.
gi 110815813   373 VSIMAGNEYVFSQLLQCKQlDLELKD 398
Cdd:pfam12796   67 YAARSGHLEIVKLLLEKGA-DINVKD 91
FYVE1_Vac1p_like cd15761
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ...
1108-1161 1.11e-05

FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277300  Cd Length: 76  Bit Score: 44.57  E-value: 1.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110815813 1108 GSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKeipIIKFDLNKPV--------RVCNICF 1161
Cdd:cd15761    10 KSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRN---RIKLNNSAEYdpkngkwcRCCEKCF 68
PHA02946 PHA02946
ankyin-like protein; Provisional
766-946 1.18e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  766 EEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVI--IQLLVSHPDIHLNVRDRQGLTP-F 842
Cdd:PHA02946   67 ETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKINNSVDEEGCGPlL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  843 ACamtfknNKSAEAILKRESG---AAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAV-QAG 918
Cdd:PHA02946  147 AC------TDPSERVFKKIMSigfEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCsKTV 220
                         170       180
                  ....*....|....*....|....*...
gi 110815813  919 SEIIVRNLLLAGAKVNELTKHRQTALHL 946
Cdd:PHA02946  221 KNVDIINLLLPSTDVNKQNKFGDSPLTL 248
PHA02874 PHA02874
ankyrin repeat protein; Provisional
214-411 1.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  214 IKSKTEYPLHKAIKVEREDVVFLYLIE-MDSQLpgkLNEADHNGDLAldlalsrrlesiaTTLVSHKADVDMVDKSGWSL 292
Cdd:PHA02874   64 INTKIPHPLLTAIKIGAHDIIKLLIDNgVDTSI---LPIPCIEKDMI-------------KTILDCGIDVNIKDAELKTF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  293 LHKGIQRGDLFAATFLIKNGAFVNAATLGAQeTPLHLvalySSKKHSADvmsemaqIAEALLQAGANPNMQDSKGRTPLH 372
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGC-YPIHI----AIKHNFFD-------IIKLLLEKGAYANVKDNNGESPLH 195
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 110815813  373 VSIMAGnEYVFSQLLQCKQLDLELKDHEGSTALWLAVQH 411
Cdd:PHA02874  196 NAAEYG-DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
758-963 1.64e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  758 PGANGeGEEEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPdIHLNVRDRQ 837
Cdd:PLN03192  513 LGDNG-GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDAN 590
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  838 GLTPFACAMTFKNNKSAEaILKRESGAAEQvdNKGRNFLHVAVQNSDIESVLFLISVHANVNSrvQDASKLTPLHLAVQA 917
Cdd:PLN03192  591 GNTALWNAISAKHHKIFR-ILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDS--EDHQGATALQVAMAE 665
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  918 GSEIIVRNLLLAGAKV--------------NELTKHRQTALHLAAQQDLPTICSVLLENG 963
Cdd:PLN03192  666 DHVDMVRLLIMNGADVdkantdddfsptelRELLQKRELGHSITIVDSVPADEPDLGRDG 725
BTB_POZ_KBTBD8 cd18274
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
61-168 1.67e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 8 (KBTBD8); KBTBD8, also called T-cell activation kelch repeat protein (TA-KRP), is a BTB-kelch family protein that is located in the Golgi apparatus and translocates to the spindle apparatus during mitosis. It acts as a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification. The BCR(KBTBD8) complex monoubiquitylates NOLC1 and its paralog TCOF1, the mutation of which underlies the neurocristopathy Treacher Collins syndrome. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349583 [Multi-domain]  Cd Length: 129  Bit Score: 45.75  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   61 LYEQEQYSDLKIKVG-DRHISAHKFVLAA-----RSDSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 134
Cdd:cd18274    16 MYDEGQLTDIVVEVDhGKTFSCHRNVLAAispyfRSMFTSGLTESTQKEVRIVGVEAESMHLVLDYAYTSRVTLTEANV- 94
                          90       100       110
                  ....*....|....*....|....*....|....
gi 110815813  135 lTELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18274    95 -QALFTAASIFQIPSLQDQCAQFMISRLDPQNSI 127
PHA02741 PHA02741
hypothetical protein; Provisional
771-852 1.68e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 46.57  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  771 GQTPLHLAA----SWGLEETVQCLLEFGANVNAQDA-EGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFACA 845
Cdd:PHA02741   60 GQMCIHIAAekheAQLAAEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139

                  ....*..
gi 110815813  846 MTFKNNK 852
Cdd:PHA02741  140 IDNEDVA 146
BTB_POZ_BTBD1_2 cd18281
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
40-136 1.88e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD1 and BTBD2; This family includes BTB/POZ domain-containing proteins BTBD1 and BTBD2, both of which are BTB-domain-containing Kelch-like proteins that interact with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349590 [Multi-domain]  Cd Length: 127  Bit Score: 45.50  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   40 QANKESSSESFisrllaivADLYEQEQYSDLKIKVG----DRHISAHKFVLAARS---DSWSLANLSSTK-ELDLSDANP 111
Cdd:cd18281     3 QASKTTVKERF--------AFLFNNETLSDVHFIVGkgdnEQRIPAHKFVLSIGSavfDAMFNGGMATTSaEIELPDVEP 74
                          90       100
                  ....*....|....*....|....*
gi 110815813  112 EVTMTMLRWIYTDELEFREDDVFLT 136
Cdd:cd18281    75 AAFLALLRFLYSDEVQIGPETVMTT 99
BTB1_POZ_ABTB1_BPOZ1 cd18295
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
50-156 2.13e-05

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1); ABTB1, also called elongation factor 1A-binding protein or bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homolog (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes. ABTB1 contains an ankyrin repeat and two BTB domains. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349604 [Multi-domain]  Cd Length: 119  Bit Score: 44.93  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   50 FISRLLaivadlyEQEQYSDLKIKVGDRHISAHKFVLAARSDSWslANLSSTK-----ELDLSDA--NPEVTMTMLRWIY 122
Cdd:cd18295     9 FLRRLL-------EQGSYSDVTFNVHGESFPAHRCILSARSPYF--AEMFETKwkdkrEINLKHPlvNPDAFRALLQYLY 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 110815813  123 TDELEFREDDVflTELMKLANRFQLQLLRERCEK 156
Cdd:cd18295    80 TGRLEIHVDDV--EDCKRLAKQCRLEELIEELEA 111
BTB_POZ_KBTBD2_BKLHD1 cd18270
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
61-170 2.18e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 2 (KBTBD2); KBTBD2, also called BTB and kelch domain-containing protein 1 (BKLHD1), plays an essential role in the regulation of insulin-signaling pathway. It is a BTB-Kelch family substrate recognition subunit of the Cullin-3-based E3 ubiquitin ligase, which targets p85alpha, the regulatory subunit of the phosphoinositol-3-kinase (PI3K) heterodimer, causing p85alpha ubiquitination and proteasome-mediated degradation. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349579 [Multi-domain]  Cd Length: 133  Bit Score: 45.38  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   61 LYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWS---LANLSSTKE--LDLSDANPEVTMTMLRWIYTDELEFREDDVfl 135
Cdd:cd18270    20 FYEQQLLTDIVLIVEGTEFPCHKMVLATCSSYFRamfMSGLSESKQthVHLRNVDAATLQIIITYAYTGNLAINDSTV-- 97
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 110815813  136 TELMKLANRFQLQLLRERCEKGVMSLVNVRNCIRF 170
Cdd:cd18270    98 EQLYETACFLQVEDVLQRCREYLIKKINAENCVRL 132
BTB_POZ_KLHL5 cd18337
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
64-168 2.55e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 5 (KLHL5); KLHL5 shares high identity and similarity with the Drosophila kelch protein, a component of ring canals. It is abundantly expressed in the ovary, adrenal gland, and thymus. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349646 [Multi-domain]  Cd Length: 130  Bit Score: 45.05  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   64 QEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTK-----ELDLSDANPEVTMTMLRWIYTDELEFREDDVFLteL 138
Cdd:cd18337    20 HKQLCDVVLVAGDRRIPAHRLVLSSVSDYFAAMFTNDVReakqeEIKMEGVEPNALWALVQYAYTGRLELKEDNIEC--L 97
                          90       100       110
                  ....*....|....*....|....*....|
gi 110815813  139 MKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18337    98 LSTACLLQLSQVVEACCKFLMKQLHPSNCL 127
PHA02859 PHA02859
ankyrin repeat protein; Provisional
881-1013 2.69e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.74  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  881 QNSDIESVLFLISVHANVNSRVQDaSKLTPLH--LAVQAGSEI-IVRNLLLAGAKVNELTKHRQTALHLAAqqdlpTICS 957
Cdd:PHA02859   62 DKVNVEILKFLIENGADVNFKTRD-NNLSALHhyLSFNKNVEPeILKILIDSGSSITEEDEDGKNLLHMYM-----CNFN 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815813  958 V-------LLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAEAFNLRGQSPLHI 1013
Cdd:PHA02859  136 VrinviklLIDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
BTB_POZ_TDPOZ cd18344
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
58-166 2.90e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in TD and POZ domain-containing proteins (TDPOZ); TDPOZ is a family of bipartite animal and plant proteins that contains a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domain. TDPOZ proteins may be nuclear scaffold proteins probably involved in transcription regulation in early development and other cellular processes. This subfamily contains only mammalian members. Plant TDPOZ proteins contain a MATH domain at the N-terminal region and are named "BTB/POZ and MATH domain-containing proteins (BPM)", not included in this subfamily. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349653 [Multi-domain]  Cd Length: 128  Bit Score: 44.95  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   58 VADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIYTDELEFREDD 132
Cdd:cd18344    14 LGELWENSLFTDCCLLVAGHEFRAHKAILAARSPVFRAMFEHEMEErlknpIEIHDLDPQVFKEMMGFIYTGKAPHLHSH 93
                          90       100       110
                  ....*....|....*....|....*....|....
gi 110815813  133 VFLTELMKLANRFQLQLLRERCEKGVMSLVNVRN 166
Cdd:cd18344    94 SMACDVLAAADKYGLEGLKVLCEDALCRNLSVEN 127
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
770-799 3.52e-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: 3.52e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 110815813    770 DGQTPLHLAASWGLEETVQCLLEFGANVNA 799
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
727-912 3.88e-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: 47.83  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  727 QTLLHRAIDENNEPTACFLIRSGCDVNSPRQ-----PGANGEGeeeARDGQTPLHLAASWGLEETVQCLLEFGA-NVNAQ 800
Cdd:cd22194   142 QTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnPKYKHEG---FYFGETPLALAACTNQPEIVQLLMEKEStDITSQ 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  801 DAEGRTPIHVAIS------SQHGVIIQL----LVSHPDIHLN-VRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVd 869
Cdd:cd22194   219 DSRGNTVLHALVTvaedskTQNDFVKRMydmiLLKSENKNLEtIRNNEGLTPLQLAAKMGKAEILKYILSREIKEKPNR- 297
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 110815813  870 NKGRNFLHVA-------------VQNSDIESVLFLISVHANVNSRvQDASKLTPLH 912
Cdd:cd22194   298 SLSRKFTDWAygpvssslydltnVDTTTDNSVLEIIVYNTNIDNR-HEMLTLEPLH 352
FYVE_CARP cd15750
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...
1111-1160 4.63e-05

FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains.


Pssm-ID: 277289 [Multi-domain]  Cd Length: 47  Bit Score: 41.96  E-value: 4.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 110815813 1111 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEipiikfdlNKPVRVCNIC 1160
Cdd:cd15750     3 CESCGAKFSVFKRKRTCADCKRYFCSNCLSKE--------ERGRRRCRRC 44
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
727-927 4.72e-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: 47.45  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  727 QTLLHRA---IDENNEPTACFLIrSGCDVNSPRQPGANGEGEEEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQdae 803
Cdd:cd22194    95 KTCLMKAllnINENTKEIVRILL-AFAEENGILDRFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAH--- 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  804 grtpihvaissQHGVIIQLLVSHPDIHLnvrdrqGLTPFACAMTFKNNKSAEAILKRESGAAEQVDNKGRNFLHVAVQNS 883
Cdd:cd22194   171 -----------AKGVFFNPKYKHEGFYF------GETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVTVA 233
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 110815813  884 D---------IESVLFLISVHANVN-SRVQDASKLTPLHLAVQAGSEIIVRNLL 927
Cdd:cd22194   234 EdsktqndfvKRMYDMILLKSENKNlETIRNNEGLTPLQLAAKMGKAEILKYIL 287
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
829-982 4.75e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 4.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   829 IHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQvdnkGRNFLHVAVQNsdIESVLFLISVHANVNSRVQDASKL 908
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLE--YVDAVEAILLHLLAAFRKSGPLEL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   909 -------------TPLHLAVQAGSEIIVRNLLLAGAKV------NELTK--------HRQTALHLAAQQDLPTICSVLLE 961
Cdd:TIGR00870  117 andqytseftpgiTALHLAAHRQNYEIVKLLLERGASVparacgDFFVKsqgvdsfyHGESPLNAAACLGSPSIVALLSE 196
                          170       180
                   ....*....|....*....|.
gi 110815813   962 NGVDFAAVDENGNNALHLAVM 982
Cdd:TIGR00870  197 DPADILTADSLGNTLLHLLVM 217
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
872-1057 5.33e-05

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: 47.31  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  872 GRNFLHVAVQNSDIESVLFLI-SVHANVNSRVqdASKL----TPLHLAVQAGSEIIVRNLLLAGAKVNeltKHRQTA--- 943
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMeAAPELVNEPM--TSDLyqgeTALHIAVVNQNLNLVRELIARGADVV---SPRATGtff 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  944 --------------LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMhgrlnnirvlltectvdaeafnlrgqs 1009
Cdd:cd22192   126 rpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL--------------------------- 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 110815813 1010 plhilgQYGKENAAAIFDLFLECMPG---YPLDK-PDADGSTVLLLAYMKGN 1057
Cdd:cd22192   179 ------QPNKTFACQMYDLILSYDKEddlQPLDLvPNNQGLTPFKLAAKEGN 224
BTB_POZ_BTBD6 cd18349
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
61-154 7.12e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 6 (BTBD6); BTBD6, also termed lens BTB domain protein, is a BTB-domain-containing Kelch-like protein required for proper embryogenesis and plays an essential evolutionary conserved role during neuronal development. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349658 [Multi-domain]  Cd Length: 109  Bit Score: 43.05  E-value: 7.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   61 LYEQEQYSDLKIKVG----DRHISAHKFVLAARSDSWS---LANLSSTK-ELDLSDANPEVTMTMLRWIYTDELEFREDD 132
Cdd:cd18349     2 MFNNELMADVHFIVGppgaSQRVPAHKYVLAVGSSVFYamfYGDLAEVKsEIHIPDVEPAAFLILLKYMYSDEIDLEADT 81
                          90       100
                  ....*....|....*....|..
gi 110815813  133 VFLTelMKLANRFQLQLLRERC 154
Cdd:cd18349    82 VLAT--LYAAKKYIVPALAKAC 101
PHA02878 PHA02878
ankyrin repeat protein; Provisional
254-409 8.40e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 8.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  254 HNGDLALDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNAATLGAQeTPLHlVALY 333
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN-TPLH-ISVG 243
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813  334 SSKKHSadvmsemaqIAEALLQAGANPNMQDS-KGRTPLHVSIMagNEYVFSQLLQCKQlDLELKDHEGSTALWLAV 409
Cdd:PHA02878  244 YCKDYD---------ILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGA-DINSLNSYKLTPLSSAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
550-798 8.75e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 8.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  550 AIAYNHPDVVSVILeqkanalhatnNLQIIPDFSLKDSRDQTVLGLALwtgMHTIAAQLLGSGAAINDTMSDG-QTLLHM 628
Cdd:PHA02875    9 AILFGELDIARRLL-----------DIGINPNFEIYDGISPIKLAMKF---RDSEAIKLLMKHGAIPDVKYPDiESELHD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  629 AIQRQDSKSALFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTL 708
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  709 VRHgcdatcwgpgpggclqtllhraidennepTACFLIRSGCdvnsprqpgangegeeeardGQTPLHLAASWGLEETVQ 788
Cdd:PHA02875  155 IDH-----------------------------KACLDIEDCC--------------------GCTPLIIAMAKGDIAICK 185
                         250
                  ....*....|
gi 110815813  789 CLLEFGANVN 798
Cdd:PHA02875  186 MLLDSGANID 195
BTB_POZ_ZBTB44 cd18228
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
52-134 9.02e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 44 (ZBTB44); ZBTB44, also called BTB/POZ domain-containing protein 15 (BTBD15) or zinc finger protein 851 (ZNF851), may be involved in transcriptional regulation. Single-nucleotide polymorphisms of ZBTB44 showed a suggestive association with disease progression of Crohn's disease. ZBTB44 has also preferentially been recognized by sera of patients with peripheral T-cell lymphoma (PTCL). It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349537 [Multi-domain]  Cd Length: 126  Bit Score: 43.31  E-value: 9.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   52 SRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDsWSLANL---SSTKELDLSDANP------EVTMT----ML 118
Cdd:cd18228     4 QELLGKLNSLRNEGHFCDVTIRVQDKIFRAHKVVLAACSD-FFRSKLvgqASPRLVLVSPAGKcvldlhHVTVTgfapLL 82
                          90
                  ....*....|....*.
gi 110815813  119 RWIYTDELEFREDDVF 134
Cdd:cd18228    83 EYAYTSTLSINTENII 98
Ank_5 pfam13857
Ankyrin repeats (many copies);
933-980 1.25e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 110815813   933 VNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLA 980
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
BTB_POZ_KLHL24_KRIP6 cd18253
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
54-167 1.55e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 24 (KLHL24); KLHL24, also called kainate receptor-interacting protein for GluR6 (KRIP6) or protein DRE1, is necessary to maintain the balance between intermediate filament stability and degradation, a process that is essential for skin integrity. KLHL24 is a component of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that mediates ubiquitination of KRT14 and controls its levels during keratinocyte differentiation. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349562 [Multi-domain]  Cd Length: 121  Bit Score: 42.51  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   54 LLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLA---NLSSTKEL--DLSDANPEVTMTMLRWIYTDELEF 128
Cdd:cd18253     5 ILQVFNEFRDSRLFTDVIICVEGREFPCHRAILSACSSYFRAMfcnDHRESREMlvEINGILAEAMDCFLQYVYTGKVKI 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 110815813  129 REDDVflTELMKLANRFQLQLLRERCEKGVMSLVNVRNC 167
Cdd:cd18253    85 TTENV--QYLFETSSLFQISPLRDACAKFLEEQLDPCNC 121
BTB_POZ_BTBD2 cd18347
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
40-154 1.96e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 2 (BTBD2); BTBD2 is a BTB-domain-containing Kelch-like protein that interacts with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349656 [Multi-domain]  Cd Length: 127  Bit Score: 42.37  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   40 QANKESSSESFisrllaivADLYEQEQYSDLKIKVGD----RHISAHKFVLAARS---DSWSLANLSSTK-ELDLSDANP 111
Cdd:cd18347     3 QATKPTVQERF--------AFLFNNEVLSDVHFLVGKglgsQRIPAHRFVLAVGSavfDAMFNGGMATTStEIELPDVEP 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 110815813  112 EVTMTMLRWIYTDELEFREDDVFLTelMKLANRFQLQLLRERC 154
Cdd:cd18347    75 AAFLALLKFLYSDEVQIGPETVMTT--LYTAKKYAVPALEAHC 115
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
869-994 2.34e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  869 DNKGRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKhrQTALHLAA 948
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVH--IRDANGNTALWNAISAKHHKIFRILYHFASISDPHAA--GDLLCTAA 630
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 110815813  949 QQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLT 994
Cdd:PLN03192  631 KRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
770-799 2.46e-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: 2.46e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 110815813   770 DGQTPLHLAASWGLEETVQCLLEFGANVNA 799
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
167-235 3.04e-04

BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are separated by as little as two residues.


Pssm-ID: 197943 [Multi-domain]  Cd Length: 101  Bit Score: 41.17  E-value: 3.04e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813    167 CIRFYQTAEELNASTLMNYCAEIIASHWDDLRK-EDFSSMSAQLLYKMIKSKTeyplhkaIKVEREDVVF 235
Cdd:smart00875    1 CLGIRRFADAHGLEELAEKALRFILQNFSEVSSsEEFLELPLEQLLELLSSDD-------LNVSSEEEVF 63
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
625-861 3.06e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 3.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   625 LLHMAIQRQDSKSALFLLEHQADINVsrtqdGETALqLAIRNQLPLVVDAIctrgADMSVPDEKGNPPLWLALAnnledi 704
Cdd:TIGR00870   56 LFVAAIENENLELTELLLNLSCRGAV-----GDTLL-HAISLEYVDAVEAI----LLHLLAAFRKSGPLELAND------ 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   705 astlvRHGCDATcwgpgPGgclQTLLHRAIDENNEPTACFLIRSGCDVN----------SPRQPGAngegeeeaRDGQTP 774
Cdd:TIGR00870  120 -----QYTSEFT-----PG---ITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSF--------YHGESP 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   775 LHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHV--------------AISSQHGVIIQLLVSHPDIHLN-VRDRQGL 839
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLlvmenefkaeyeelSCQMYNFALSLLDKLRDSKELEvILNHQGL 258
                          250       260
                   ....*....|....*....|..
gi 110815813   840 TPFACAMTFKNNKSAEAILKRE 861
Cdd:TIGR00870  259 TPLKLAAKEGRIVLFRLKLAIK 280
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
350-410 3.39e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 3.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110815813  350 AEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQlDLELKDHEGSTALWLAVQ 410
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLELAEE 157
BTB_POZ_KLHL12_C3IP1_DKIR cd18242
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
47-167 3.47e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 12 (KLHL12); KLHL12, also called CUL3-interacting protein 1 (C3IP1) or DKIR homolog, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of the Wnt signaling pathway and ER-Golgi transport. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349551 [Multi-domain]  Cd Length: 124  Bit Score: 41.66  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   47 SESFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSD------SWSLANlSSTKELDLSDANPEVTMTMLRW 120
Cdd:cd18242     1 TNSHAKSILNTMNSLRKSNTLCDVTLRVEGKEFPAHRIVLAACSDyfcamfTSEMSE-KGKSEVELQGLTASTMEILLDF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 110815813  121 IYTDELEFREDDVflTELMKLANRFQLQLLRERCEKGVMSLVNVRNC 167
Cdd:cd18242    80 VYTETVHVTVENV--QELLPAACLLQLKGVKQACCEFLESQLDPSNC 124
BTB_POZ_BAB-like cd18315
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
67-146 3.60e-04

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster proteins bric-a-brac 1 (BAB1), bric-a-brac 2 (BAB2), modifier of mdg4 (doom), and similar proteins; BAB1 and BAB2 probably act as transcriptional regulators that are required for specification of the tarsal segment and are involved in antenna development. Doom is a product of the Drosophila mod(mdg4) gene. It induces apoptosis and binds to baculovirus inhibitor-of-apoptosis proteins. This subfamily also includes Drosophila melanogaster sex determination protein fruitless (FRU), protein jim lovell (LOV), zinc finger protein chinmo, transcription factor GAGA, transcription factor Ken, and longitudinals lacking proteins (LOLA). FRU probably acts as a transcriptional regulator that plays a role in male courtship behavior and sexual orientation, and enhances male-specific expression of takeout in brain-associated fat body. LOV, also called tyrosine kinase-related (TKR), has a regulatory role during midline cell development. Chinmo is a functional effector of the JAK/STAT pathway that regulates eye development, tumor formation, and stem cell self-renewal in Drosophila. GAGA is a transcriptional activator that functions by regulating chromatin structure. Ken, also termed protein Ken and Barbie, is a transcription factor required for Terminalia development. LOLA proteins are putative transcription factors required for axon growth and guidance in the central and peripheral nervous systems. Proteins in this subfamily contain a BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349624 [Multi-domain]  Cd Length: 85  Bit Score: 40.61  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   67 YSDLKIKVGDRHISAHKFVLAARSDSWS--LANLSSTKELDLS--DANPEVTMTMLRWIYTDELEFREDDvfLTELMKLA 142
Cdd:cd18315     1 LVDVTLACEGGSLKAHKLVLAAASPYFAalLKETPPDEHPVIIlpDVPYSELKALLDFIYTGEVNVSQEQ--LESLLKLA 78

                  ....
gi 110815813  143 NRFQ 146
Cdd:cd18315    79 ELLQ 82
BTB_POZ_KLHL2-like cd18235
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
52-154 4.16e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins, KLHL2 and KLHL3; The family includes Kelch-like proteins, KLHL2 and KLHL3. KLHL2 is a novel actin-binding protein predominantly expressed in brain. It plays a role in the reorganization of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors. KLHL2 and KLHL3 each functions as a component of an E3 ubiquitin ligase complex that mediates the ubiquitination of target proteins. They contain a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349544 [Multi-domain]  Cd Length: 121  Bit Score: 41.26  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   52 SRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW-----SLANLSSTKELDLSDANPEVTMTMLRWIYTDEL 126
Cdd:cd18235     6 QKAFDVMNELRKQNLLCDVILVADGVEIPAHRVVLASCSPYFhamftGDLSESRANRVTLQDVDGKALLLLIDYVYTAEI 85
                          90       100
                  ....*....|....*....|....*...
gi 110815813  127 EFREDDVflTELMKLANRFQLQLLRERC 154
Cdd:cd18235    86 QVTEENV--QVLLPAANLLQLTDVRDAC 111
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
727-861 4.56e-04

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 44.41  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  727 QTLLHRAIDENNEPTACFLIRSGCDVNSprqpGANGEGEEEARD------GQTPLHLAASWGLEETVQCLLE---FGANV 797
Cdd:cd22196    95 QTALHIAIERRNMHLVELLVQNGADVHA----RASGEFFKKKKGgpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADI 170
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110815813  798 NAQDAEGRTPIH--VAISSQ------------HGVIIQLLVSHPDIHL-NVRDRQGLTPFACAMTFKNNKSAEAILKRE 861
Cdd:cd22196   171 SARDSMGNTVLHalVEVADNtpentkfvtkmyNEILILGAKIRPLLKLeEITNKKGLTPLKLAAKTGKIGIFAYILGRE 249
Ank_5 pfam13857
Ankyrin repeats (many copies);
769-811 4.76e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.76e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 110815813   769 RDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVA 811
Cdd:pfam13857   14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02736 PHA02736
Viral ankyrin protein; Provisional
769-845 5.19e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.79  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  769 RDGQTPLHLAASWGL---EETVQCLLEFGANVNAQDA-EGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFAC 844
Cdd:PHA02736   53 RHGKQCVHIVSNPDKadpQEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYV 132

                  .
gi 110815813  845 A 845
Cdd:PHA02736  133 A 133
PHA02875 PHA02875
ankyrin repeat protein; Provisional
219-361 5.52e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 5.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  219 EYPLHKAikVEREDVVFLYLIEMDSQLPGKLNEADHNGDLALdLALSRRLEsIATTLVSHKADVDMVDKSGWSLLHKGIQ 298
Cdd:PHA02875   69 ESELHDA--VEEGDVKAVEELLDLGKFADDVFYKDGMTPLHL-ATILKKLD-IMKLLIARGADPDIPNTDKFSPLHLAVM 144
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815813  299 RGDLFAATFLIKNGAFVNAATlGAQETPLhLVALysSKKHSAdvmsemaqIAEALLQAGANPN 361
Cdd:PHA02875  145 MGDIKGIELLIDHKACLDIED-CCGCTPL-IIAM--AKGDIA--------ICKMLLDSGANID 195
Ank_5 pfam13857
Ankyrin repeats (many copies);
790-842 7.55e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 7.55e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 110815813   790 LLEFG-ANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPdIHLNVRDRQGLTPF 842
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTAL 53
BTB_POZ_calicin cd18307
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
67-154 7.55e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in calicin; Calicin is a basic cytoskeletal protein involved in the formation and maintenance of the highly regular organization of the postacrosomal perinuclear theca, the calyx of mammalian spermatozoa. It contains BTB and BACK domains at the N-terminal region and kelch repeats at the C-terminal region. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349616 [Multi-domain]  Cd Length: 97  Bit Score: 39.79  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   67 YSDLKIKVGDRHISAHKFVLAARS----DSWSLANLSSTKEL----DLSDANPEVTMTMLRWIYTDELEFREDDVflTEL 138
Cdd:cd18307     1 FCDVVISVDNHSFAAHRNVLAAVSpfvkSLISSNDMKATDELsitiDCDYLSPETVEQLLDYFYTGKIVISEKNV--EDL 78
                          90
                  ....*....|....*.
gi 110815813  139 MKLANRFQLQLLRERC 154
Cdd:cd18307    79 LKGAKYFNIPRLKDHC 94
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
776-845 7.62e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 7.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110815813  776 HLAASwGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQH-GVIIQLLVSHPDIHLnvRDRQGLTPFACA 845
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHvQVVRVLLEFGADPTL--LDKDGKTPLELA 155
PHA02875 PHA02875
ankyrin repeat protein; Provisional
476-684 8.57e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 8.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  476 FLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGanpnlqteealplpkeaasltSLADSVHLQ---TPLHMAIA 552
Cdd:PHA02875   53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG---------------------KFADDVFYKdgmTPLHLATI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  553 YNHPDVVSVILEQKANalhatnnlqiiPDFSLKDSrdQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQR 632
Cdd:PHA02875  112 LKKLDIMKLLIARGAD-----------PDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110815813  633 QDSKSALFLLEHQADIN-VSRTQDgETALQLAIRNQLPLVVDAICTRGADMSV 684
Cdd:PHA02875  179 GDIAICKMLLDSGANIDyFGKNGC-VAALCYAIENNKIDIVRLFIKRGADCNI 230
BTB_POZ_ARIA_plant cd18352
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
61-155 9.44e-04

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in plant ARM repeat protein interacting with ABF2 (ARIA) and similar proteins; ARIA is an armadillo (ARM) repeat and BTB domain-containing protein that acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2, a transcription factor which controls ABA-dependent gene expression via the G-box-type ABA-responsive elements. ARIA is a novel abscisic acid signaling component. It negatively regulates seed germination and young seedling growth. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349661 [Multi-domain]  Cd Length: 116  Bit Score: 40.15  E-value: 9.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   61 LYEQEQY------SDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELDLSDAN-P----EVTMTMLRWIYTDELEFR 129
Cdd:cd18352     1 VYLGEQYvnnatlSDVTFLVEGRRFYAHRIALLASSDAFRAMFDGGYREKEARDIEiPnirwEVFELMMRFIYTGSVDIT 80
                          90       100
                  ....*....|....*....|....*.
gi 110815813  130 EDDVFltELMKLANRFQLQLLRERCE 155
Cdd:cd18352    81 NDIAK--DLLRAADQYLLEGLKRLCE 104
BTB_POZ_KLHL3 cd18339
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
49-154 9.94e-04

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 3 (KLHL3); KLHL3 is a component of an E3 ubiquitin ligase complex that regulates blood pressure by targeting With-No-Lysine (WNK) kinases for degradation. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349648 [Multi-domain]  Cd Length: 121  Bit Score: 40.47  E-value: 9.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   49 SFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSL-----ANLSSTKELDLSDANPEVTMTMLRWIYT 123
Cdd:cd18339     3 AHMKKAFKVMNELRSKQLLCDVTIVAEDVEIEAHRVVLAACSPYFCAmftgdMSESKAKKIEIKDVDGQTLSKLIDYIYT 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 110815813  124 DELEFREDDVFLteLMKLANRFQLQLLRERC 154
Cdd:cd18339    83 AEIEVTEENVQV--LLPAASLLQLMDVRQNC 111
BTB_POZ_KLHL21 cd18250
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
54-167 1.01e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 21 (KLHL21); KLHL21 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for efficient chromosome alignment and cytokinesis. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of aurora B. KLHL21 also targets IkappaB kinase-beta to regulate nuclear factor kappa-light chain enhancer of activated B cells (NF-kappaB) signaling negatively. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349559 [Multi-domain]  Cd Length: 124  Bit Score: 40.14  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   54 LLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLA-----NLSSTKELDLSDANPEVTMTMLRWIYTDELEF 128
Cdd:cd18250     8 LLRGLSELRAERKFFDVTLCAGGREFPCHRTVLAAASSYFRAMfagelRESRADRVVLHGVSAEILGLLLDFSYTGRVTV 87
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 110815813  129 REDDVFLteLMKLANRFQLQLLRERCEKGVMSLVNVRNC 167
Cdd:cd18250    88 TQDNVEA--LLRAADLFQFPSVKEACCAYLQQRLDVSNC 124
PHA02875 PHA02875
ankyrin repeat protein; Provisional
505-715 1.05e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  505 NLTAELLQQGANPNLQTEEALPLPKEAASLTslaDSVHLQTPL-HMAIA-YNHPDVVS----VILEQKANALHATNNL-Q 577
Cdd:PHA02875   16 DIARRLLDIGINPNFEIYDGISPIKLAMKFR---DSEAIKLLMkHGAIPdVKYPDIESelhdAVEEGDVKAVEELLDLgK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  578 IIPDFSLKDSrdQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsrtQD-- 655
Cdd:PHA02875   93 FADDVFYKDG--MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI---EDcc 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110815813  656 GETALQLAIRNQLPLVVDAICTRGADmsvPDEKGNPP----LWLALANNLEDIASTLVRHGCDA 715
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGADC 228
PHA02798 PHA02798
ankyrin-like protein; Provisional
703-965 1.15e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  703 DIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNE-PTACFLIRSGCDVNsprqpgangegeEEARDGQTPLHLAASW 781
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDYKHMlDIVKILIENGADIN------------KKNSDGETPLYCLLSN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  782 GL---EETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV---IIQLLV-SHPDIHLnVRDRQGLTPFACAMTFKNNKSA 854
Cdd:PHA02798  120 GYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLeKGVDINT-HNNKEKYDTLHCYFKYNIDRID 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  855 EAILKR--ESGAAEQVDNKG--RNFLHVAVQ----NSDIES-VLFLISVHANVNSRvqDASKLTPLHLAVQAGSEIIVRN 925
Cdd:PHA02798  199 ADILKLfvDNGFIINKENKShkKKFMEYLNSllydNKRFKKnILDFIFSYIDINQV--DELGFNPLYYSVSHNNRKIFEY 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 110815813  926 LLLAGAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVD 965
Cdd:PHA02798  277 LLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
Ank_5 pfam13857
Ankyrin repeats (many copies);
484-525 1.34e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 110815813   484 VNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEAL 525
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL 50
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
289-408 1.34e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  289 GWSLLHKGIQRGDLFAATFLIKNGAFVNAATLGA------------QETPLHLVALYSSKkhsadvmsemaQIAEALLQA 356
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgnlfyfGELPLSLAACTNQE-----------EIVRLLLEN 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  357 GANP---NMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLDL---------------ELKDHEGSTALWLA 408
Cdd:cd21882   142 GAQPaalEAQDSLGNTVLHALVLQADNTPENSAFVCQMYNLllsygahldptqqleEIPNHQGLTPLKLA 211
BTB_POZ_NPR_plant cd18310
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
64-150 1.78e-03

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in plant regulatory proteins, NPR1-4, and similar proteins; NPR1 and NPR2 are essential for pathogenicity and the utilization of many nitrogen sources. NPR1 is also called nitrogen pathogenicity regulation protein NPR1, non-inducible immunity protein 1 (Nim1), nonexpresser of PR genes 1, or salicylic acid insensitive 1 (Sai1). It acts as a transcription coactivator that plays dual roles in regulating plant immunity. NPR3 and NPR4 are involved in negative regulation of defense responses against pathogens in plant. NPR proteins contain a BTB domain, DUF3420, ankyrin (ANK) repeats, and a conserved C-terminal domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349619 [Multi-domain]  Cd Length: 145  Bit Score: 39.98  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   64 QEQYSDLKIKVGD-RHISAHKFVLAARSDS-----WSLANLSSTK--ELDLSDANP------EVTMTMLRWIYTDELEFR 129
Cdd:cd18310    15 DLFYSDAEIIVEGgRPVPVHRCILAARSPFfrdifASAKAEGANTkpKLELRELIPggivgyDAFMLVLSYLYSGRLRLV 94
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 110815813  130 EDDV------------------FLTELMKLANRFQLQLL 150
Cdd:cd18310    95 PKEGsacvdsdcwhvacrpavdFALEVLYAASVFQIPEL 133
PHA02884 PHA02884
ankyrin repeat protein; Provisional
703-811 1.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.89  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  703 DIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegEEEARdgQTPLHLAASWG 782
Cdd:PHA02884   47 DIIDAILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRY---------AEEAK--ITPLYISVLHG 115
                          90       100
                  ....*....|....*....|....*....
gi 110815813  783 LEETVQCLLEFGANVNAQDAEGRTPIHVA 811
Cdd:PHA02884  116 CLKCLEILLSYGADINIQTNDMVTPIELA 144
PHA02859 PHA02859
ankyrin repeat protein; Provisional
307-373 2.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 2.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815813  307 FLIKNGAFVNAATLGAQETPLHLVALYSSkkhsaDVMSEMAQIaeaLLQAGANPNMQDSKGRTPLHV 373
Cdd:PHA02859   71 FLIENGADVNFKTRDNNLSALHHYLSFNK-----NVEPEILKI---LIDSGSSITEEDEDGKNLLHM 129
Ank_5 pfam13857
Ankyrin repeats (many copies);
613-663 2.17e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 110815813   613 AAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLA 663
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
251-410 2.29e-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: 42.05  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  251 EADHNGDLALDLALSRRLESIATTLVSHKADVDMVDKsgwsllhkgiqrGDLFAATFliKNGAFVNAatlgaqETPLHLV 330
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAK------------GVFFNPKY--KHEGFYFG------ETPLALA 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  331 ALysskkhsadvmSEMAQIAEALLQAGANP-NMQDSKGRTPLHVSIMAG------NEYVFSQ----LLQCKQLDLE-LKD 398
Cdd:cd22194   196 AC-----------TNQPEIVQLLMEKESTDiTSQDSRGNTVLHALVTVAedsktqNDFVKRMydmiLLKSENKNLEtIRN 264
                         170
                  ....*....|..
gi 110815813  399 HEGSTALWLAVQ 410
Cdd:cd22194   265 NEGLTPLQLAAK 276
BTB_POZ cd01165
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
71-145 2.38e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain superfamily; Proteins in this superfamily are characterized by the presence of a common protein-protein interaction motif of about 100 amino acids, known as the BTB/POZ domain. Members include transcription factors, oncogenic proteins, ion channel proteins, and potassium channel tetramerization domain (KCTD) proteins. They have been identified in poxviruses and many eukaryotes, and have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats, among others. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. In ion channel proteins and KCTD proteins, the BTB/POZ domain is also called the tetramerization (T1) domain.


Pssm-ID: 349496 [Multi-domain]  Cd Length: 79  Bit Score: 38.03  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   71 KIKVGDRHISAHKFVLAARS-----DSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVFltELMKLANRF 145
Cdd:cd01165     2 VLVVEGEKFHVNKELLAQSSeyfraLFRGGFRESGQAEINLRDISPEDFRALLEFLYGGKRDLDASNLL--ELLEAANFL 79
Ank_5 pfam13857
Ankyrin repeats (many copies);
895-947 2.39e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 110815813   895 HANVNSRVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLA 947
Cdd:pfam13857    4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
BTB_POZ_ZBTB40 cd18225
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
49-147 2.76e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 40 (ZBTB40); ZBTB40 may be involved in transcriptional regulation. Single-nucleotide polymorphisms of ZBTB40 are associated with bone mineral density in European and East-Asian populations. ZBTB40 contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349534 [Multi-domain]  Cd Length: 116  Bit Score: 39.04  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   49 SFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW-SLANLSSTKELDLSDANPEVTMTMLRWIYTDELE 127
Cdd:cd18225     5 NYSRQLLQQLHTLRKEQQFCDCTIFIGTFHFRAHKLVLAASSLLFkSLLDSTDTISIDASVVSPEEFALLLEMVYTGKLP 84
                          90       100
                  ....*....|....*....|
gi 110815813  128 FREDDvfLTELMKLANRFQL 147
Cdd:cd18225    85 PGKHN--FTKIISVADSLQM 102
BTB_POZ_KLHL38 cd18268
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
48-168 3.09e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 38 (KLHL38); KLHL38 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. Its function remains unclear. The KLHL38 gene is significantly up-regulated during diapause, a temporary arrest of development during early ontogeny. It may also function in preadipocyte differentiation in the chicken. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349577 [Multi-domain]  Cd Length: 129  Bit Score: 39.00  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   48 ESFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIY 122
Cdd:cd18268     4 QDLSSELLRQLNSLRQERILTDVILCTGDKEIPCHRNVLASSSPYFRAMFCNNFREssqakVDLKGIDSDVLDQIVDYVY 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 110815813  123 TDELEFREDDVFltELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18268    84 TGEILITRDNVL--PLMEAASMLQYPKLFEACSLYLQDQLTPENCL 127
Ank_4 pfam13637
Ankyrin repeats (many copies);
259-309 3.21e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 3.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 110815813   259 ALDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLI 309
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
BTB2_POZ_IBtk cd18302
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
68-166 3.55e-03

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in inhibitor of Bruton tyrosine kinase (IBtk); IBtk is an inhibitor or negative regulator of Bruton tyrosine kinase (Btk), which is required for B-cell differentiation and development. IBtk binds to the PH domain of Btk and down-regulates the Btk kinase activity. It contains two BTB domains. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349611 [Multi-domain]  Cd Length: 113  Bit Score: 38.50  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   68 SDLKIKVGD-RHISAHKFVLAARSD------SWSLANLSSTKELDLsDANPEVTMTMLRWIYTDE---LEFREDDVFLTE 137
Cdd:cd18302     6 YDVTIVSEDgKEFPCHKCVLVARLEyfhsmlSSSWIEASSCSALTM-PIPSDILEIILDYLYTDEasaVKESQNVEFLCN 84
                          90       100
                  ....*....|....*....|....*....
gi 110815813  138 LMKLANRFQLQLLRERCEKGVMSLVNVRN 166
Cdd:cd18302    85 VLVIADQLLITRLKEICEVALVELLSLKN 113
PHA03095 PHA03095
ankyrin-like protein; Provisional
221-396 3.67e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  221 PLHKAIKVEREDVVFL-YLIEMDSqlpgKLNEADHNGDLALD-LALSRRL-ESIATTLVSHKADVDMVDKSGWSLLHK-- 295
Cdd:PHA03095  155 PLAVLLKSRNANVELLrLLIDAGA----DVYAVDDRFRSLLHhHLQSFKPrARIVRELIRAGCDPAATDMLGNTPLHSma 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  296 ---GIQRGDLFaatFLIKNGAFVNAATLGAQeTPLHLVALYSSKkhsadvmseMAqiAEALLQAGANPNMQDSKGRTPLH 372
Cdd:PHA03095  231 tgsSCKRSLVL---PLLIAGISINARNRYGQ-TPLHYAAVFNNP---------RA--CRRLIALGADINAVSSDGNTPLS 295
                         170       180
                  ....*....|....*....|....
gi 110815813  373 VSIMAGNEYVFSQLLQcKQLDLEL 396
Cdd:PHA03095  296 LMVRNNNGRAVRAALA-KNPSAET 318
BTB_POZ_BTBD12_SLX4 cd18288
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
51-155 4.35e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Structure-specific endonuclease subunit SLX4; SLX4, also called BTB/POZ domain-containing protein 12 (BTBD12), is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases and is required for DNA repair. Mutations of the SLX4 gene are found in Fanconi anemia. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349597 [Multi-domain]  Cd Length: 116  Bit Score: 38.21  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   51 ISRLLAIVADLYEQEQYSDLKIKV-GDRHISAHKFVLAAR---------SDSWSLAN--LSSTKELDLSDANPEVTMTML 118
Cdd:cd18288     2 LGKLAADFSAMVNNPHLSDVQFQTdSGEVLYAHSFVLYARcplliqmvhSEGFSVEEegGVTTRRVLLGDVSGEAARCFL 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 110815813  119 RWIYTDELEFREDdvFLTELMKLANRFQLQLLRERCE 155
Cdd:cd18288    82 QYLYTADTGLPPG--LSPHVSELADRFGVSELVHLCE 116
BTB_POZ_ABTB2_BPOZ2 cd18350
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
68-168 5.37e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2); ABTB2, also called bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins with various functions ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. It inhibits the aggregation of alpha-synuclein, with implications for Parkinson's disease. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation, and prevent translation. It is also involved in the growth suppressive effect of the phosphatase and tensin homolog (PTEN). It contains an ankyrin repeat, BTB/POZ, and BACK domains. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349659 [Multi-domain]  Cd Length: 134  Bit Score: 38.29  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   68 SDLKIKVGDRHISAHKFVLAARSDSWS--LANLS-----STKELDLSDANPEVTMTMLRWIY---TDELEFREDDVFltE 137
Cdd:cd18350    25 SDVTFLVEGKLFYAHKVLLVTASNRFKslLTNKSeqesqGSKTIEISDIKYHIFQMLMQYLYyggTESMEIPIADVL--E 102
                          90       100       110
                  ....*....|....*....|....*....|.
gi 110815813  138 LMKLANRFQLQLLRERCEKGVMSLVNVRNCI 168
Cdd:cd18350   103 LLSAASLFQLDALQRHCEILCSQTINLENAV 133
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
909-1031 5.37e-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: 40.90  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  909 TPLHLAVQAGSEIIVRNLLLAGAKVNELTKHR--------------QTALHLAAQQDLPTICSVLLENG-VDFAAVDENG 973
Cdd:cd22194   143 TALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKEsTDITSQDSRG 222
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110815813  974 NNALHLAVM-----HGRLNNIRVLLTECTVDAEAFNL------RGQSPLHILGQYGKenaAAIFDLFLE 1031
Cdd:cd22194   223 NTVLHALVTvaedsKTQNDFVKRMYDMILLKSENKNLetirnnEGLTPLQLAAKMGK---AEILKYILS 288
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
491-519 5.54e-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: 35.64  E-value: 5.54e-03
                            10        20
                    ....*....|....*....|....*....
gi 110815813    491 GETPLHTACRHGLANLTAELLQQGANPNL 519
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
BTB_POZ_KBTBD11 cd18275
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
69-167 5.81e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 11 (KBTBD11); KBTBD11 is also called chronic myelogenous leukemia-associated protein (CMLAP) or Kelch domain-containing protein 7B, or KLHDC7C. It is a BTB-Kelch family protein whose function remains unclear. A novel polymorphism rs11777210 in KBTBD11 is significantly associated with colorectal cancer risk. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349584 [Multi-domain]  Cd Length: 104  Bit Score: 37.47  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   69 DLKIKVGDRHISAHKFVLAARSDSWSlANLSStKELDLSDANPEVTMTMLRWIYTDELEFREDDVflTELMKLANRFQLQ 148
Cdd:cd18275     6 DLVIEVSGQRIRAHKSVLAAKSDYFR-ARLSR-DILKVKGLSYATLRLLVDYVYSGRMAVSKDNV--VEVVAGARFLQMP 81
                          90
                  ....*....|....*....
gi 110815813  149 LLRERCEKGVMSLVNVRNC 167
Cdd:cd18275    82 CAAQCAVDAVRAQLCLGNC 100
BTB2_POZ_ABTB1_BPOZ1 cd18296
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
67-156 5.87e-03

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1); ABTB1, also called elongation factor 1A-binding protein or bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homolog (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes. ABTB1 contains an ankyrin repeat and two BTB domains. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349605 [Multi-domain]  Cd Length: 121  Bit Score: 38.05  E-value: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813   67 YSDLKIKVGDRHISAHKFVLAARSD----------SWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVFlt 136
Cdd:cd18296    17 FPDVCFQVEGHRFPCHKAFFCGRSDyfkallrdhfAESEENNGSIPVVTLHDVSPEVFAIVLYYIYTDDTDLPPENAY-- 94
                          90       100
                  ....*....|....*....|
gi 110815813  137 ELMKLANRFQLQLLRERCEK 156
Cdd:cd18296    95 DVLYVADMYLLPGLKRLCGT 114
BTB1_POZ_BTBD8 cd18285
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
61-123 7.18e-03

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 8 (BTBD8); BTBD8 is a BTB-domain-containing Kelch-like protein that may play a role in developmental processes. It may also act as a protein-protein adaptor in a transcription complex and thus be involved in brain development. BTBD8 contains two BTB domains. This model corresponds to the first domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349594 [Multi-domain]  Cd Length: 104  Bit Score: 37.33  E-value: 7.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110815813   61 LYEQEQYSDLKIKVGDRHISAHKFVLAARSD---SWSLANLSSTKELDLSD-ANPEVT--MTMLRWIYT 123
Cdd:cd18285     9 LLREELHTDVTFYVGSTLFKAHKAILLARVPeffSHIIGKLSSLEDQEPINiENLEASefKTFLRQVYT 77
Ank_4 pfam13637
Ankyrin repeats (many copies);
872-927 7.27e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 7.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 110815813   872 GRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLL 927
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADIN--AVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
876-1086 7.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  876 LHVAVQNSDIESVLFLISVHAN-VNSRVQDASklTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPT 954
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETT--TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  955 ICSVLLENGVDFA------------------AVDENGNNA-----LHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPL 1011
Cdd:PHA02874   83 IIKLLIDNGVDTSilpipciekdmiktildcGIDVNIKDAelktfLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPI 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815813 1012 HILGqygKENAAAIFDLFLEcmpgypldkpdadgstvlllaymkgnanlcraivrSGARLGVNNNQGVNIFNYQV 1086
Cdd:PHA02874  162 HIAI---KHNFFDIIKLLLE-----------------------------------KGAYANVKDNNGESPLHNAA 198
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
909-1019 9.18e-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: 40.16  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  909 TPLHLAVQAGSEIIVRNLLLAGAKVNELTKHR--------------QTALHLAAQQDLPTICSVLLENG---VDFAAVDE 971
Cdd:cd22193    78 TALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENEhqpADIEAQDS 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815813  972 NGNNALHLAVM---HGRLNNIRV------LLTEC-----TVDAEA-FNLRGQSPLHILGQYGK 1019
Cdd:cd22193   158 RGNTVLHALVTvadNTKENTKFVtrmydmILIRGaklcpTVELEEiRNNDGLTPLQLAAKMGK 220
PHA02946 PHA02946
ankyin-like protein; Provisional
607-814 9.31e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 9.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  607 QLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRTQDGETALQLA-IRNQLPLVVDAICTRGADMSVP 685
Cdd:PHA02946   57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSgTDDEVIERINLLVQYGAKINNS 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815813  686 -DEKGNPPLwLALANNLEDIASTLVRHGCDATC---WGpgpggclQTLLHRAIDENN--EPTACFLIRSGCdvnSPRQPG 759
Cdd:PHA02946  137 vDEEGCGPL-LACTDPSERVFKKIMSIGFEARIvdkFG-------KNHIHRHLMSDNpkASTISWMMKLGI---SPSKPD 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 110815813  760 angegeeeaRDGQTPLHLAASWGLEET-VQCLLEFGANVNAQDAEGRTPIHVAISS 814
Cdd:PHA02946  206 ---------HDGNTPLHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT 252
Ank_4 pfam13637
Ankyrin repeats (many copies);
728-791 9.59e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 9.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110815813   728 TLLHRAIDENNEPTACFLIRSGCDVNspRQPGangegeeearDGQTPLHLAASWGLEETVQCLL 791
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADIN--AVDG----------NGETALHFAASNGNVEVLKLLL 54
 
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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