NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767992314|ref|XP_011522228|]
View 

rabankyrin-5 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
92-211 2.81e-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: 218.73  E-value: 2.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   92 FISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFR 171
Cdd:cd18303     1 FISRLLKTVASLFDKELYSDITIKLADKSIPAHKFVLAARSEKWSNENLASTNELDLSDISYEVVLALLRWLYTDELDLT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767992314  172 EDDVFLTELMKLANRFQLQLLRERCEKGVMSLVNVRNCIR 211
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 ...
204-292 4.70e-54

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: 182.84  E-value: 4.70e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  204 VNVRNCIRFYQTAEELNASTLMNYCAEIIASHWDDLRKEDFSSMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEM 283
Cdd:cd18501     1 VNVRNCIRFYQTAEEIGASTLREYCSEIISTHWDDLTPEDFAKMSAPLLYRMFKSKTKHPLHAAIRLKREDVVFLYLIEF 80

                  ....*....
gi 767992314  284 DSQLPGKLN 292
Cdd:cd18501    81 DSQLPGKLN 89
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
1144-1206 4.05e-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: 159.13  E-value: 4.05e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767992314 1144 EPPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1206
Cdd:cd15728     1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
681-1019 1.33e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 1.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  681 LFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcw 760
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  761 gpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVN 840
Cdd:COG0666    82 --AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR------------DKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  841 AQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHV 920
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETP----------------------------------LHL 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  921 AVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSV 1000
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVN--AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 767992314 1001 LLENGVDFAAVDENGNNAL 1019
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-747 2.04e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 2.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  476 FDENSFAARLIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQ 555
Cdd:COG0666    30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  556 GANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVL 635
Cdd:COG0666   110 GADVNARDKDG-------------------ETPLHLAAYNGNLEIVKLLLEAGA-------------DVNAQDNDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  636 GLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAIRNQLPLVVD 715
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVK 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767992314  716 AICTRGADMSVPDEKGNPPLWLALANNLEDIA 747
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
246-597 1.26e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  246 SMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEMDSQLPGKLNEADHNGDLALDLALSRRLESIATTLVSHKADVD 325
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  326 MVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNaATLGAQETPLHLVALYSSKKhsadvmsemaqIAEALLQAGANPNMQ 405
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLE-----------IVKLLLEAGADVNAQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  406 DSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLELKDHEGSTALWLAVQHitvssdqsvnpfEDVPVVNgtsfdensfaarl 485
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAEN------------GHLEIVK------------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  486 iqrgshtdapdtatgncllqraagagneaaalFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEE 565
Cdd:COG0666   204 --------------------------------LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
                         330       340       350
                  ....*....|....*....|....*....|..
gi 767992314  566 ALPLPKEAASLTSLADSVHLQTPLHMAIAYNH 597
Cdd:COG0666   252 GLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
Ank_2 pfam12796
Ankyrin repeats (3 copies);
986-1065 5.63e-11

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 5.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   986 LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAeafNLRGQSPLHILGQYGKENAA 1065
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 ...
92-211 2.81e-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: 218.73  E-value: 2.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   92 FISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFR 171
Cdd:cd18303     1 FISRLLKTVASLFDKELYSDITIKLADKSIPAHKFVLAARSEKWSNENLASTNELDLSDISYEVVLALLRWLYTDELDLT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767992314  172 EDDVFLTELMKLANRFQLQLLRERCEKGVMSLVNVRNCIR 211
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 ...
204-292 4.70e-54

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: 182.84  E-value: 4.70e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  204 VNVRNCIRFYQTAEELNASTLMNYCAEIIASHWDDLRKEDFSSMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEM 283
Cdd:cd18501     1 VNVRNCIRFYQTAEEIGASTLREYCSEIISTHWDDLTPEDFAKMSAPLLYRMFKSKTKHPLHAAIRLKREDVVFLYLIEF 80

                  ....*....
gi 767992314  284 DSQLPGKLN 292
Cdd:cd18501    81 DSQLPGKLN 89
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
1144-1206 4.05e-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: 159.13  E-value: 4.05e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767992314 1144 EPPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1206
Cdd:cd15728     1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
681-1019 1.33e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 1.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  681 LFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcw 760
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  761 gpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVN 840
Cdd:COG0666    82 --AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR------------DKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  841 AQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHV 920
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETP----------------------------------LHL 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  921 AVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSV 1000
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVN--AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 767992314 1001 LLENGVDFAAVDENGNNAL 1019
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-747 2.04e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 2.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  476 FDENSFAARLIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQ 555
Cdd:COG0666    30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  556 GANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVL 635
Cdd:COG0666   110 GADVNARDKDG-------------------ETPLHLAAYNGNLEIVKLLLEAGA-------------DVNAQDNDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  636 GLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAIRNQLPLVVD 715
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVK 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767992314  716 AICTRGADMSVPDEKGNPPLWLALANNLEDIA 747
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
1145-1206 8.10e-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: 98.66  E-value: 8.10e-25
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767992314   1145 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1206
Cdd:smart00064    2 PHWIPDEEvsnCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDCYENL 66
PHA03095 PHA03095
ankyrin-like protein; Provisional
745-1036 2.06e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 105.11  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  745 DIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNEpTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWG 824
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD-IVRLLLEAGADVNAP------------ERCGFTPLHLYLYNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  825 LEETV-QCLLEFGANVNAQDAEGRTPIHVAISSQ--HGVIIQLLVSHpDIHLNVRDRQGLTPFACAMtfKNNKSAEAILK 901
Cdd:PHA03095   95 TTLDViKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRK-GADVNALDLYGMTPLAVLL--KSRNANVELLR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  902 R--ESGAAE-QVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAVQAGS--EIIVRNLLLAGAKVN 976
Cdd:PHA03095  172 LliDAGADVyAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISIN 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  977 ELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHgrlNNIRVLLT 1036
Cdd:PHA03095  252 ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN---NNGRAVRA 308
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
246-597 1.26e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  246 SMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEMDSQLPGKLNEADHNGDLALDLALSRRLESIATTLVSHKADVD 325
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  326 MVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNaATLGAQETPLHLVALYSSKKhsadvmsemaqIAEALLQAGANPNMQ 405
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLE-----------IVKLLLEAGADVNAQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  406 DSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLELKDHEGSTALWLAVQHitvssdqsvnpfEDVPVVNgtsfdensfaarl 485
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAEN------------GHLEIVK------------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  486 iqrgshtdapdtatgncllqraagagneaaalFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEE 565
Cdd:COG0666   204 --------------------------------LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
                         330       340       350
                  ....*....|....*....|....*....|..
gi 767992314  566 ALPLPKEAASLTSLADSVHLQTPLHMAIAYNH 597
Cdd:COG0666   252 GLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
1145-1207 1.61e-22

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: 92.06  E-value: 1.61e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314  1145 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPII-KFDLNKPVRVCNICFDVLT 1207
Cdd:pfam01363    1 PVWVPDSSatvCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpELGSNKPVRVCDACYDTLQ 67
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
111-198 6.33e-17

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: 77.35  E-value: 6.33e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314    111 DLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELD-----LSDANPEVTMTMLRWIYTDELEFREDDVFltELMKLAN 185
Cdd:smart00225    1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDkseiyLDDVSPEDFRALLNFLYTGKLDLPEENVE--ELLELAD 78
                            90
                    ....*....|...
gi 767992314    186 RFQLQLLRERCEK 198
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 ...
102-198 1.40e-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: 76.53  E-value: 1.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   102 DLYEQEQYSDLKIKVGDRHISAHKFVLAARSDS-WSLANL----SSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 176
Cdd:pfam00651    3 ELREQGELCDVTLVVGDKEFRAHKAVLAACSPYfKALFSGqeseSSVSEITLDDVSPEDFEALLEFMYTGKLISEENVD- 81
                           90       100
                   ....*....|....*....|..
gi 767992314   177 ltELMKLANRFQLQLLRERCEK 198
Cdd:pfam00651   82 --DLLAAADKLQIPSLVDKCEE 101
Ank_2 pfam12796
Ankyrin repeats (3 copies);
918-1012 6.40e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 6.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   918 LHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRnLLLAGAKVNELTKHRqTALHLAAQQDLPTI 997
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDNGR-TALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 767992314   998 CSVLLENGVDFAAVD 1012
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
349-622 2.37e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  349 FLIKNGAFVNAATL-GAqeTPLHLVALYSSKkhsADVMsemaqiaEALLQAGANPNMQDSKGRTPLHV--SIMAGNEYVF 425
Cdd:PHA03095   68 LLLEAGADVNAPERcGF--TPLHLYLYNATT---LDVI-------KLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  426 SQLLQcKQLDLELKDHEGSTALwlavqHITVSS------------DQSVNPFeDVPVVNGTSFDE--NSFAAR------L 485
Cdd:PHA03095  136 RLLLR-KGADVNALDLYGMTPL-----AVLLKSrnanvellrlliDAGADVY-AVDDRFRSLLHHhlQSFKPRarivreL 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  486 IQRGSHTDAPDtATGNCLLQRAAGAGNEAAAL---FLAtNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQ 562
Cdd:PHA03095  209 IRAGCDPAATD-MLGNTPLHSMATGSSCKRSLvlpLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314  563 TEEALplpkeaasltsladsvhlqTPLHMAIAYNHPDVVSVILEQK------ANAL-HATNNLQIIP 622
Cdd:PHA03095  287 SSDGN-------------------TPLSLMVRNNNGRAVRAALAKNpsaetvAATLnTASVAGGDIP 334
Ank_2 pfam12796
Ankyrin repeats (3 copies);
986-1065 5.63e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 5.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   986 LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAeafNLRGQSPLHILGQYGKENAA 1065
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
769-887 9.09e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 66.19  E-value: 9.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  769 QTLLHRAIDENNEPTACFLIRSGCDVNSPRqpgANGEGEEEARD-----GQTPLHLAASWGLEETVQCLLEFGANVNAQD 843
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVSPR---ATGTFFRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767992314  844 AEGRTPIHVAISSQHGV----IIQLLVSHpDIHLN------VRDRQGLTPFACA 887
Cdd:cd22192   167 SLGNTVLHILVLQPNKTfacqMYDLILSY-DKEDDlqpldlVPNNQGLTPFKLA 219
PHA03100 PHA03100
ankyrin repeat protein; Provisional
254-432 1.71e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  254 KMIKSKTEYPLHKAIK-VEREDVVFLYLIemdSQLPGKLNEADHNGDLALDLALSRRLES--IATTLVSHKADVDMVDKS 330
Cdd:PHA03100   64 STKNNSTPLHYLSNIKyNLTDVKEIVKLL---LEYGANVNAPDNNGITPLLYAISKKSNSysIVEYLLDNGANVNIKNSD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  331 GWSLLH---KGIQRgDLFAATFLIKNGAFVNAAT-------LGAQ--------ETPLHLVALYSSKkhsadvmsemaQIA 392
Cdd:PHA03100  141 GENLLHlylESNKI-DLKILKLLIDKGVDINAKNrvnyllsYGVPinikdvygFTPLHYAVYNNNP-----------EFV 208
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767992314  393 EALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCK 432
Cdd:PHA03100  209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
PHA03100 PHA03100
ankyrin repeat protein; Provisional
943-1121 2.33e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  943 RVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQ-----DLPTICSVLLENGVDFAAVDENGNN 1017
Cdd:PHA03100   29 DYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGIT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314 1018 ALHLAVMHgRLNNIRV--LLTECTVDAEAFNLRGQSPLHILGQYGKE---------------NAAAIFDLFLECmpGYPL 1080
Cdd:PHA03100  109 PLLYAISK-KSNSYSIveYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdiNAKNRVNYLLSY--GVPI 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767992314 1081 DKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGV 1121
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
518-610 1.29e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.20  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   518 FLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQgANPNLQTEEalplpkeaasltsladsvhlQTPLHMAIAYNH 597
Cdd:pfam12796   15 LLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG--------------------RTALHYAARSGH 73
                           90
                   ....*....|...
gi 767992314   598 PDVVSVILEQKAN 610
Cdd:pfam12796   74 LEIVKLLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
384-453 3.55e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 3.55e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   384 VMSEMAQIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLDLelkDHEGSTALWLAVQH 453
Cdd:pfam12796    5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARS 71
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
812-841 2.82e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.82e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 767992314    812 DGQTPLHLAASWGLEETVQCLLEFGANVNA 841
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
871-1024 4.51e-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: 4.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   871 IHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQvdnkGRNFLHVAVQNsdIESVLFLISVHANVNSRVQDASKL 950
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLE--YVDAVEAILLHLLAAFRKSGPLEL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   951 -------------TPLHLAVQAGSEIIVRNLLLAGAKV------NELTK--------HRQTALHLAAQQDLPTICSVLLE 1003
Cdd:TIGR00870  117 andqytseftpgiTALHLAAHRQNYEIVKLLLERGASVparacgDFFVKsqgvdsfyHGESPLNAAACLGSPSIVALLSE 196
                          170       180
                   ....*....|....*....|.
gi 767992314  1004 NGVDFAAVDENGNNALHLAVM 1024
Cdd:TIGR00870  197 DPADILTADSLGNTLLHLLVM 217
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
209-277 2.33e-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: 41.56  E-value: 2.33e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314    209 CIRFYQTAEELNASTLMNYCAEIIASHWDDLRK-EDFSSMSAQLLYKMIKSKTeyplhkaIKVEREDVVF 277
Cdd:smart00875    1 CLGIRRFADAHGLEELAEKALRFILQNFSEVSSsEEFLELPLEQLLELLSSDD-------LNVSSEEEVF 63
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
331-450 1.18e-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: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  331 GWSLLHKGIQRGDLFAATFLIKNGAFVNAATLGA------------QETPLHLVALYSSKkhsadvmsemaQIAEALLQA 398
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgnlfyfGELPLSLAACTNQE-----------EIVRLLLEN 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  399 GANP---NMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLDL---------------ELKDHEGSTALWLA 450
Cdd:cd21882   142 GAQPaalEAQDSLGNTVLHALVLQADNTPENSAFVCQMYNLllsygahldptqqleEIPNHQGLTPLKLA 211
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
533-561 4.62e-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: 4.62e-03
                            10        20
                    ....*....|....*....|....*....
gi 767992314    533 GETPLHTACRHGLANLTAELLQQGANPNL 561
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 ...
92-211 2.81e-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: 218.73  E-value: 2.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   92 FISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFR 171
Cdd:cd18303     1 FISRLLKTVASLFDKELYSDITIKLADKSIPAHKFVLAARSEKWSNENLASTNELDLSDISYEVVLALLRWLYTDELDLT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767992314  172 EDDVFLTELMKLANRFQLQLLRERCEKGVMSLVNVRNCIR 211
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 ...
204-292 4.70e-54

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: 182.84  E-value: 4.70e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  204 VNVRNCIRFYQTAEELNASTLMNYCAEIIASHWDDLRKEDFSSMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEM 283
Cdd:cd18501     1 VNVRNCIRFYQTAEEIGASTLREYCSEIISTHWDDLTPEDFAKMSAPLLYRMFKSKTKHPLHAAIRLKREDVVFLYLIEF 80

                  ....*....
gi 767992314  284 DSQLPGKLN 292
Cdd:cd18501    81 DSQLPGKLN 89
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
1144-1206 4.05e-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: 159.13  E-value: 4.05e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767992314 1144 EPPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1206
Cdd:cd15728     1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
681-1019 1.33e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 1.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  681 LFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcw 760
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  761 gpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVN 840
Cdd:COG0666    82 --AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR------------DKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  841 AQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHV 920
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETP----------------------------------LHL 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  921 AVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSV 1000
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVN--AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 767992314 1001 LLENGVDFAAVDENGNNAL 1019
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
832-1120 1.20e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  832 LLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVD 911
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  912 NKGRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQ 991
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVN--ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  992 QDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPLHILGQYGKENAAAIFDLF 1071
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767992314 1072 LEcmpgyPLDKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQG 1120
Cdd:COG0666   242 GA-----DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
611-917 8.51e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 8.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  611 ALHATNNLQIIPDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADI 690
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  691 NVsRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATCWGPGpggcLQT 770
Cdd:COG0666    81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND----GNT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  771 LLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPI 850
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNAR------------DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314  851 HVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVDNKGRNF 917
Cdd:COG0666   224 DLAAENGNLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
646-950 3.44e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.82  E-value: 3.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  646 IAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRtQDGETALQLAIRNQLPLVVDAICTRGADMS 725
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALAD-ALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  726 VPDEKGNPPLWLALANNLEDIASTLVRHGCDATcwgpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgange 805
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  806 geeeARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPFA 885
Cdd:COG0666   150 ----DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALD 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767992314  886 CAMTFKNNKSAEAILKREsGAAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKL 950
Cdd:COG0666   225 LAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-747 2.04e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 2.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  476 FDENSFAARLIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQ 555
Cdd:COG0666    30 LLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  556 GANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVL 635
Cdd:COG0666   110 GADVNARDKDG-------------------ETPLHLAAYNGNLEIVKLLLEAGA-------------DVNAQDNDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  636 GLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAIRNQLPLVVD 715
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVK 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 767992314  716 AICTRGADMSVPDEKGNPPLWLALANNLEDIA 747
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
1145-1206 8.10e-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: 98.66  E-value: 8.10e-25
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767992314   1145 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1206
Cdd:smart00064    2 PHWIPDEEvsnCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDCYENL 66
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
1147-1206 9.51e-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: 98.23  E-value: 9.51e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314 1147 WCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1206
Cdd:cd15720     2 WKDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFGIEKEVRVCDPCYEKL 61
PHA03095 PHA03095
ankyrin-like protein; Provisional
745-1036 2.06e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 105.11  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  745 DIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNEpTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWG 824
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD-IVRLLLEAGADVNAP------------ERCGFTPLHLYLYNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  825 LEETV-QCLLEFGANVNAQDAEGRTPIHVAISSQ--HGVIIQLLVSHpDIHLNVRDRQGLTPFACAMtfKNNKSAEAILK 901
Cdd:PHA03095   95 TTLDViKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRK-GADVNALDLYGMTPLAVLL--KSRNANVELLR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  902 R--ESGAAE-QVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAVQAGS--EIIVRNLLLAGAKVN 976
Cdd:PHA03095  172 LliDAGADVyAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISIN 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  977 ELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHgrlNNIRVLLT 1036
Cdd:PHA03095  252 ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN---NNGRAVRA 308
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
246-597 1.26e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  246 SMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEMDSQLPGKLNEADHNGDLALDLALSRRLESIATTLVSHKADVD 325
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  326 MVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNaATLGAQETPLHLVALYSSKKhsadvmsemaqIAEALLQAGANPNMQ 405
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLE-----------IVKLLLEAGADVNAQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  406 DSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLELKDHEGSTALWLAVQHitvssdqsvnpfEDVPVVNgtsfdensfaarl 485
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAEN------------GHLEIVK------------- 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  486 iqrgshtdapdtatgncllqraagagneaaalFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEE 565
Cdd:COG0666   204 --------------------------------LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251
                         330       340       350
                  ....*....|....*....|....*....|..
gi 767992314  566 ALPLPKEAASLTSLADSVHLQTPLHMAIAYNH 597
Cdd:COG0666   252 GLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
1145-1207 1.61e-22

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: 92.06  E-value: 1.61e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314  1145 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPII-KFDLNKPVRVCNICFDVLT 1207
Cdd:pfam01363    1 PVWVPDSSatvCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpELGSNKPVRVCDACYDTLQ 67
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
220-453 4.04e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 4.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  220 NASTLMNYCAEIIASHWDDLRKEDFSSMSAQLLYKMIKSKTEYPLHKAIKVEREDVVFLYLIEMDSqlpgkLNEADHNGD 299
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD-----INAKDDGGN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  300 LALDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNAATlGAQETPLHLVALYSSKK 379
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLE 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767992314  380 hsadvmsemaqIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLELKDHEGSTALWLAVQH 453
Cdd:COG0666   168 -----------IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE-AGADVNAKDNDGKTALDLAAEN 229
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-735 5.06e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 5.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  477 DENSFAARLIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQG 556
Cdd:COG0666    64 AGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  557 ANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLG 636
Cdd:COG0666   144 ADVNAQDNDG-------------------NTPLHLAAANGNLEIVKLLLEAGA-------------DVNARDNDGETPLH 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  637 LALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAIRNQLPLVVDA 716
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA-KDKDGLTALLLAAAAGAALIVKL 270
                         250
                  ....*....|....*....
gi 767992314  717 ICTRGADMSVPDEKGNPPL 735
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
545-865 1.72e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.18  E-value: 1.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  545 LANLTAELLQQGANPNLQTEEALPLPKEAASLTSLADSVHLQTPLHMAIAYNHPDVVSVILEQKANALHATNNLQIIPDF 624
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  625 SLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQL 704
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  705 AIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcwgpgpggclqtllhrAIDENnepta 784
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN----------------AKDND----- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  785 cflirsgcdvnsprqpgangegeeeardGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQL 864
Cdd:COG0666   219 ----------------------------GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                  .
gi 767992314  865 L 865
Cdd:COG0666   271 L 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
278-617 1.53e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  278 LYLIEMDSQLPGKLNEADHNGDLALDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLIKNGAFV 357
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  358 NAATLGaQETPLHLVALYSSKKhsadvmsemaqIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLE 437
Cdd:COG0666    81 NAKDDG-GNTLLHAAARNGDLE-----------IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  438 LKDHEGSTALWLAVQHitvssdqsvnpfEDVPVVNgtsfdensfaarliqrgshtdapdtatgncllqraagagneaaal 517
Cdd:COG0666   148 AQDNDGNTPLHLAAAN------------GNLEIVK--------------------------------------------- 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  518 FLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNH 597
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG-------------------KTALDLAAENGN 231
                         330       340
                  ....*....|....*....|
gi 767992314  598 PDVVSVILEQKANALHATNN 617
Cdd:COG0666   232 LEIVKLLLEAGADLNAKDKD 251
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
1153-1203 8.21e-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: 83.74  E-value: 8.21e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767992314 1153 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1203
Cdd:cd00065     2 CMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSGKPVRVCDSCY 52
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
1145-1203 7.56e-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: 81.42  E-value: 7.56e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767992314 1145 PPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1203
Cdd:cd15735     1 PEWVDSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQPVRVCDGCY 59
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
1144-1204 1.11e-18

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: 81.24  E-value: 1.11e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767992314 1144 EPP-W---CDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFD 1204
Cdd:cd15731     1 DPPlWvpdEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGQMKPVRVCNHCFM 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
896-1126 2.72e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 2.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  896 AEAILKRESGAAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKV 975
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  976 NELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPLHI 1055
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992314 1056 LGQYGKEnaaAIFDLFLECmpGYPLDKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGVNIFNY 1126
Cdd:COG0666   160 AAANGNL---EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
PHA02876 PHA02876
ankyrin repeat protein; Provisional
830-1054 2.76e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 90.51  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  830 QCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAaeq 909
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI--- 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  910 vdNKGRNFLHVAVQNSDIESVLFLISVHANVNSrvQDASKLTPLHLAVQAGS-EIIVRNLLLAGAKVNELTKHRQTALHL 988
Cdd:PHA02876  238 --NKNDLSLLKAIRNEDLETSLLLYDAGFSVNS--IDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYL 313
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314  989 AAQQDLPTI-CSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAEAFNLRGQSPLH 1054
Cdd:PHA02876  314 MAKNGYDTEnIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIH 380
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
1145-1206 4.42e-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: 79.36  E-value: 4.42e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767992314 1145 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlnKPVRVCNICFDVL 1206
Cdd:cd15730     1 RKWADDEEvqnCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSK--KPVRVCDACFDDL 63
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
1144-1202 1.61e-17

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: 77.80  E-value: 1.61e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767992314 1144 EPPW---CDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNIC 1202
Cdd:cd15727     1 EPPWvpdKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPRMCFVDPVRVCNEC 62
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
1150-1206 3.28e-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: 77.04  E-value: 3.28e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314 1150 GSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 1206
Cdd:cd15719     9 GDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRISRPVRVCQACYNIL 65
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
109-187 3.56e-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: 77.21  E-value: 3.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  109 YSDLKIKVGDRHISAHKFVLAARSD-----SWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVFltELMKL 183
Cdd:cd18186     1 LCDVTLVVGGREFPAHRAVLAARSPyframFSSGMKESSSSEIELDDVSPEAFEALLDYIYTGELELSEENVE--ELLAA 78

                  ....
gi 767992314  184 ANRF 187
Cdd:cd18186    79 ADKL 82
PHA03095 PHA03095
ankyrin-like protein; Provisional
827-1121 4.69e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 4.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  827 ETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV---IIQLLVSHpDIHLNVRDRQGLTPFACAMTFKNnksAEAILKR- 902
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEA-GADVNAPERCGFTPLHLYLYNAT---TLDVIKLl 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  903 -ESGA-AEQVDNKGRNFLHV--AVQNSDIESVLFLISVHANVNSRvqDASKLTPLH-LAVQAGSEI-IVRNLLLAGAKVN 976
Cdd:PHA03095  104 iKAGAdVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNAL--DLYGMTPLAvLLKSRNANVeLLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  977 ELTKHRQTALHLAAQ--QDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRvlltectvdaeafnlrgqsplh 1054
Cdd:PHA03095  182 AVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSL---------------------- 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314 1055 ilgqygkenaaaIFDLFLEcmpGYPLDKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGV 1121
Cdd:PHA03095  240 ------------VLPLLIA---GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
111-198 6.33e-17

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: 77.35  E-value: 6.33e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314    111 DLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELD-----LSDANPEVTMTMLRWIYTDELEFREDDVFltELMKLAN 185
Cdd:smart00225    1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDkseiyLDDVSPEDFRALLNFLYTGKLDLPEENVE--ELLELAD 78
                            90
                    ....*....|...
gi 767992314    186 RFQLQLLRERCEK 198
Cdd:smart00225   79 YLQIPGLVELCEE 91
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
1151-1203 1.01e-16

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: 75.16  E-value: 1.01e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767992314 1151 SYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1203
Cdd:cd15733     8 SHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQLYDPVRVCNSCY 60
PHA02874 PHA02874
ankyrin repeat protein; Provisional
690-1048 1.08e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.24  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  690 INVSrTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATCWgPGPggclq 769
Cdd:PHA02874   28 INIS-VDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL-PIP----- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  770 tllhraiDENNEpTACFLIRSGCDVNSprqpgangegeeEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTP 849
Cdd:PHA02874  101 -------CIEKD-MIKTILDCGIDVNI------------KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  850 IHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHVAVQNSDIES 929
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEK-GAYANVKDNNGESP----------------------------------LHNAAEYGDYAC 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  930 VLFLISVHANVNSRVQDAskLTPLHLAVQAGSEIIvrNLLLAGAKVNELTKHRQTALHLAAQQDLPT-ICSVLLENGVDF 1008
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNG--FTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADI 281
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 767992314 1009 AAVDENGNNALHLAVMH-GRLNNIRVLLTECTVDAEAFNLR 1048
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 ...
102-198 1.40e-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: 76.53  E-value: 1.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   102 DLYEQEQYSDLKIKVGDRHISAHKFVLAARSDS-WSLANL----SSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 176
Cdd:pfam00651    3 ELREQGELCDVTLVVGDKEFRAHKAVLAACSPYfKALFSGqeseSSVSEITLDDVSPEDFEALLEFMYTGKLISEENVD- 81
                           90       100
                   ....*....|....*....|..
gi 767992314   177 ltELMKLANRFQLQLLRERCEK 198
Cdd:pfam00651   82 --DLLAAADKLQIPSLVDKCEE 101
PHA02874 PHA02874
ankyrin repeat protein; Provisional
815-1059 1.91e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.47  E-value: 1.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  815 TPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVshpdihLNVRDRQGLtPFACAmtfkNNK 894
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI------DNGVDTSIL-PIPCI----EKD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  895 SAEAILkrESGAAEQV-DNKGRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGA 973
Cdd:PHA02874  106 MIKTIL--DCGIDVNIkDAELKTFLHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  974 KVNELTKHRQTALHLAAQQ-DLPTIcSVLLENGVDFAAVDENGNNALHLAVMHGRlNNIRVLLTECTVDAEAFNlrGQSP 1052
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYgDYACI-KLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDID--GSTP 257

                  ....*..
gi 767992314 1053 LHILGQY 1059
Cdd:PHA02874  258 LHHAINP 264
PHA03100 PHA03100
ankyrin repeat protein; Provisional
666-871 2.18e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  666 TLLHMAIQRQDSKSALFLLEHQADINVSRTQDgETAL-----QLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALA 740
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNN-STPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  741 NNLED--IASTLVRHGCDA---TCWGPGP------GGC-----LQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgang 804
Cdd:PHA03100  116 KKSNSysIVEYLLDNGANVnikNSDGENLlhlyleSNKidlkiLKLLIDKGVDINAKNRVNYLLSYGVPINIK------- 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  805 egeeearD--GQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSH-PDI 871
Cdd:PHA03100  189 -------DvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNgPSI 251
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
1146-1203 2.74e-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: 73.87  E-value: 2.74e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767992314 1146 PWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKF-DLNKPVRVCNICF 1203
Cdd:cd15760     1 HWKPDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPHLgPLGVPQRVCDRCF 59
PHA02876 PHA02876
ankyrin repeat protein; Provisional
646-1059 8.11e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.42  E-value: 8.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  646 IAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSrTQDGETALQLAIRNQLPLVVDAICtrgadms 725
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNII-ALDDLSVLECAVDSKNIDTIKAII------- 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  726 vpDEKGNPplwlalanNLEDIAstlvrhgcdatcwgpgpggclqtlLHRAIDENNEPTACFLIRSGCDVNSPrqpgange 805
Cdd:PHA02876  232 --DNRSNI--------NKNDLS------------------------LLKAIRNEDLETSLLLYDAGFSVNSI-------- 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  806 geEEARDgqTPLHLAA-SWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV--IIQLLVSHPDIhlNVRDRQGLT 882
Cdd:PHA02876  270 --DDCKN--TPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTenIRTLIMLGADV--NAADRLYIT 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  883 PFACAMTFKNNKsaeailkresgaaeqvdnkgrnflhvavqnsdiESVLFLISVHANVNSRvqDASKLTPLHLAVQAGSE 962
Cdd:PHA02876  344 PLHQASTLDRNK---------------------------------DIVITLLELGANVNAR--DYCDKTPIHYAAVRNNV 388
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  963 IIVRNLLLAGAKVNELTKHRQTALHLAAQQDLP-TICSVLLENGVDFAAVDENGNNALHLAVMHG-RLNNIRVLLtECTV 1040
Cdd:PHA02876  389 VIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLL-DNGA 467
                         410
                  ....*....|....*....
gi 767992314 1041 DAEAFNLRGQSPLHILGQY 1059
Cdd:PHA02876  468 DVNAINIQNQYPLLIALEY 486
BTB_POZ_trishanku-like cd18314
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
104-196 1.01e-15

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: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  104 YEQEQYSDLKIKVGDRHISAHKFVLAARSDSWS---LANL--SSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVFlt 178
Cdd:cd18314     1 YNDSEFSDVVLCVGDRKFFAHRIVLCARSPVFRsmlTGSMieSNLKEVTLEDVEPEIFETVLKYMYTGQVTLSEENVL-- 78
                          90
                  ....*....|....*...
gi 767992314  179 ELMKLANRFQLQLLRERC 196
Cdd:cd18314    79 DLLMLASKYQVPDLEKLC 96
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
103-198 2.55e-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: 73.05  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  103 LYEQEQYSDLKIKVGDR--HISAHKFVLAARSDSWS------LANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDD 174
Cdd:cd18294     8 LINNPEFSDVKFLVGPErqEIFAHKCILAARCEVFRamfltgPQKESTQSPLVLSDIEPEVFRAVLEFIYTNCVTLSNHT 87
                          90       100
                  ....*....|....*....|....
gi 767992314  175 VFltELMKLANRFQLQLLRERCEK 198
Cdd:cd18294    88 VI--EVLAAAVEYGLDELRKLCER 109
Ank_2 pfam12796
Ankyrin repeats (3 copies);
918-1012 6.40e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 6.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   918 LHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRnLLLAGAKVNELTKHRqTALHLAAQQDLPTI 997
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDNGR-TALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 767992314   998 CSVLLENGVDFAAVD 1012
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
1149-1207 1.98e-14

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: 69.29  E-value: 1.98e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767992314 1149 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPiiKFDLNKPVRVCNICFDVLT 1207
Cdd:cd15739     9 DVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVP--SGPNRRPARVCDVCHTLLV 65
PHA02878 PHA02878
ankyrin repeat protein; Provisional
816-1055 2.80e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.84  E-value: 2.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  816 PLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVShpdihLNVRDRQGLTPFACAMTFKNNKS 895
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR-----SINKCSVFYTLVAIKDAFNNRNV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  896 --AEAILKRESGAAEQVDNKgrnFLHVAVQNSDIES--VLFLISVHANVNSRVQDASKlTPLHLAVQAGSEIIVRNLLLA 971
Cdd:PHA02878  115 eiFKIILTNRYKNIQTIDLV---YIDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSY 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  972 GAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVmhGRLNNIRVL--LTECTVDAEAFN-LR 1048
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKDYDILklLLEHGVDVNAKSyIL 268

                  ....*..
gi 767992314 1049 GQSPLHI 1055
Cdd:PHA02878  269 GLTALHS 275
Ank_2 pfam12796
Ankyrin repeats (3 copies);
817-943 4.03e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 4.03e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   817 LHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIhlnvrdrqgltpfacamtfknnksa 896
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV------------------------- 55
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 767992314   897 eailkresgaaeQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSR 943
Cdd:pfam12796   56 ------------NLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
1153-1203 9.21e-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: 66.96  E-value: 9.21e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767992314 1153 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1203
Cdd:cd15725    11 CYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCC 61
Ank_2 pfam12796
Ankyrin repeats (3 copies);
953-1035 1.06e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 1.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   953 LHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSVLLENGvdFAAVDENGNNALHLAVMHGRLNNIR 1032
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGHLEIVK 78

                   ...
gi 767992314  1033 VLL 1035
Cdd:pfam12796   79 LLL 81
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
1153-1203 1.31e-13

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: 66.25  E-value: 1.31e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767992314 1153 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFdlNKPVRVCNICF 1203
Cdd:cd15721    10 CQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSS--AKPVRVCDTCY 58
FYVE_WDFY1_like cd15718
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ...
1145-1203 2.08e-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: 66.19  E-value: 2.08e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767992314 1145 PPWCDGSYCYECTARF-----------GVTTRKHHCRHCGRLLCHKCSTKE--IPIIKFDLnkPVRVCNICF 1203
Cdd:cd15718     1 PEWAESDNCQKCSRPFfwnfkqmwekkTLGVRQHHCRKCGKAVCDKCSSNRstIPVMGFEF--PVRVCNECY 70
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
1149-1206 2.98e-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: 65.86  E-value: 2.98e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767992314 1149 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlnKPVRVCNICFDVL 1206
Cdd:cd15758    11 EATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYP--KPVRVCDSCHTLL 66
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
1153-1203 3.19e-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: 65.31  E-value: 3.19e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767992314 1153 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1203
Cdd:cd15732    11 CYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQLFEPSRVCKSCF 61
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
1143-1206 4.78e-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: 65.07  E-value: 4.78e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767992314 1143 KEPP-WC---DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTkeipiIKFDL----NKPVRVCNICFDVL 1206
Cdd:cd15729     2 KVAPvWVpdsEAPNCMQCEVKFTFTKRRHHCRACGKVLCSACCS-----LKARLeyldNKEARVCVPCYQTL 68
PHA02874 PHA02874
ankyrin repeat protein; Provisional
629-931 7.21e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.30  E-value: 7.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  629 SRDQTVLGL--ALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRTQDgetalqlaI 706
Cdd:PHA02874   31 SVDETTTPLidAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPC--------I 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  707 RNQLplvVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATCwgPGPGGCLQtlLHRAIDENNEPTACF 786
Cdd:PHA02874  103 EKDM---IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI--EDDNGCYP--IHIAIKHNFFDIIKL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  787 LIRSGCDVNSprqpgangegeeEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIiQLLV 866
Cdd:PHA02874  176 LLEKGAYANV------------KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI-ELLI 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767992314  867 SHPDIhlNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVDNKGRNFLHVAVQNSDIESVL 931
Cdd:PHA02874  243 NNASI--NDQDIDGSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVI 305
PHA02875 PHA02875
ankyrin repeat protein; Provisional
809-1007 7.78e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.95  E-value: 7.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  809 EARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFACAM 888
Cdd:PHA02875   31 EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLAT 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  889 TFKNNKSAEAILKResGAAEQVDNKGR-NFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRN 967
Cdd:PHA02875  111 ILKKLDIMKLLIAR--GADPDIPNTDKfSPLHLAVMMGDIKGIELLIDHKACLD--IEDCCGCTPLIIAMAKGDIAICKM 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767992314  968 LLLAGAKVNELTKHRQ-TALHLAAQQDLPTICSVLLENGVD 1007
Cdd:PHA02875  187 LLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
1153-1206 2.63e-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: 2.63e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314 1153 CYECT-ARFGVTTRKHHCRHCGRLLCHKCSTKE--IPIIKfdlNKPVRVCNICFDVL 1206
Cdd:cd15754    11 CMRCTqTNFSLLTRRHHCRKCGFVVCHECSRQRflIPRLS---PKPVRVCSLCYRKL 64
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
1153-1203 2.86e-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: 62.74  E-value: 2.86e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767992314 1153 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1203
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), ...
1153-1203 3.11e-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: 62.77  E-value: 3.11e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767992314 1153 CYECT-ARFGVTTRKHHCRHCGRLLCHKCSTKeipiiKFDL----NKPVRVCNICF 1203
Cdd:cd15717    11 CMHCKkTKFTAINRRHHCRKCGAVVCGACSSK-----KFLLphqsSKPLRVCDTCY 61
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
1146-1203 4.55e-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: 62.07  E-value: 4.55e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767992314 1146 PWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlNKPVRVCNICF 1203
Cdd:cd15743     5 PDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPLEYLK-NKSARVCDECF 61
PHA02876 PHA02876
ankyrin repeat protein; Provisional
519-865 5.67e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.09  E-value: 5.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  519 LATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEALplpkeaasltsladsvhlqTPLHMAIAYNHP 598
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDL-------------------SVLECAVDSKNI 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  599 DVVSVILEQKANA-------LHATNNLQIIPDFSLKDSR---------DQTVLGLALWT-GMHTIAAQLLGSGAAINDTM 661
Cdd:PHA02876  225 DTIKAIIDNRSNInkndlslLKAIRNEDLETSLLLYDAGfsvnsiddcKNTPLHHASQApSLSRLVPKLLERGADVNAKN 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  662 SDGQTLLH-MAIQRQDSKSALFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALA 740
Cdd:PHA02876  305 IKGETPLYlMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAV 384
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  741 NNLEDIASTLVRHGCDATCWGPGPGgclqTLLHRAIDENNEPTAC-FLIRSGCDVNSprqpgangegeeEARDGQTPLHL 819
Cdd:PHA02876  385 RNNVVIINTLLDYGADIEALSQKIG----TALHFALCGTNPYMSVkTLIDRGANVNS------------KNKDLSTPLHY 448
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 767992314  820 AASWGLE-ETVQCLLEFGANVNAQDAEGRTPIHVAIsSQHGVIIQLL 865
Cdd:PHA02876  449 ACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL-EYHGIVNILL 494
BTB2_POZ_RhoBTB cd18300
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
109-197 1.26e-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: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  109 YSDLKIKVGDRHISAHKFVLAARSDsWSLANL------SSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVFLtELMK 182
Cdd:cd18300     9 FSDVTFIVEDGTIPAHKALLVARCD-VMAAMFggnfreSSAKEVELPGVSKETFLALLEYLYTDQAPILEDGDCV-GLIV 86
                          90
                  ....*....|....*
gi 767992314  183 LANRFQLQLLRERCE 197
Cdd:cd18300    87 LANRLCLPRLVALCE 101
PHA03100 PHA03100
ankyrin repeat protein; Provisional
770-1014 1.60e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.77  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  770 TLLHRAIDENNEPTACFLIRSGCDVNSprqpgangegeeEARDGQTPLHLAASWGLE-----ETVQCLLEFGANVNAQDA 844
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINS------------STKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  845 EGRTPIHVAIS--SQHGVIIQLLVSHpdihlnvrdrqgltpfACAMTFKNNKsaeailkresgaaeqvdnkGRNFLHVAV 922
Cdd:PHA03100  105 NGITPLLYAISkkSNSYSIVEYLLDN----------------GANVNIKNSD-------------------GENLLHLYL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  923 QNSDIES--VLFLISVHANVNSR--------------VQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTAL 986
Cdd:PHA03100  150 ESNKIDLkiLKLLIDKGVDINAKnrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
                         250       260
                  ....*....|....*....|....*...
gi 767992314  987 HLAAQQDLPTICSVLLENGVDFAAVDEN 1014
Cdd:PHA03100  230 HIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
349-622 2.37e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  349 FLIKNGAFVNAATL-GAqeTPLHLVALYSSKkhsADVMsemaqiaEALLQAGANPNMQDSKGRTPLHV--SIMAGNEYVF 425
Cdd:PHA03095   68 LLLEAGADVNAPERcGF--TPLHLYLYNATT---LDVI-------KLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  426 SQLLQcKQLDLELKDHEGSTALwlavqHITVSS------------DQSVNPFeDVPVVNGTSFDE--NSFAAR------L 485
Cdd:PHA03095  136 RLLLR-KGADVNALDLYGMTPL-----AVLLKSrnanvellrlliDAGADVY-AVDDRFRSLLHHhlQSFKPRarivreL 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  486 IQRGSHTDAPDtATGNCLLQRAAGAGNEAAAL---FLAtNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQ 562
Cdd:PHA03095  209 IRAGCDPAATD-MLGNTPLHSMATGSSCKRSLvlpLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314  563 TEEALplpkeaasltsladsvhlqTPLHMAIAYNHPDVVSVILEQK------ANAL-HATNNLQIIP 622
Cdd:PHA03095  287 SSDGN-------------------TPLSLMVRNNNGRAVRAALAKNpsaetvAATLnTASVAGGDIP 334
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
1146-1206 2.76e-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: 60.05  E-value: 2.76e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767992314 1146 PWCDGS---YCYECTARFGVTTRKHHCRHCGRLLCHKCStkeipiiKFdLNKPVRVCNICFDVL 1206
Cdd:cd15716     3 PWVNDSdvpFCPDCGKKFNLARRRHHCRLCGSIMCNKCS-------QF-LPLHIRCCHHCKDLL 58
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
1146-1206 3.01e-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: 3.01e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767992314 1146 PWCDGSYCYECT-ARFGVTTRKHHCRHCGRLLCHKCSTKEIpIIKFDLNKPVRVCNICFDVL 1206
Cdd:cd15755     4 PDSEATVCMRCQkAKFTPVNRRHHCRKCGFVVCGPCSEKKF-LLPSQSSKPVRVCDFCYDLL 64
PHA03100 PHA03100
ankyrin repeat protein; Provisional
909-1076 3.29e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 3.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  909 QVDNKGRNFLH-----VAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQA--GSEIIVRNLLLAGAKVNELTKH 981
Cdd:PHA03100   63 SSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN--APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  982 RQTALHLAAQQDLPT--ICSVLLENGVDFAA----------------VDENGNNALHLAVMHGRLNNIRVLLtECTVDAE 1043
Cdd:PHA03100  141 GENLLHLYLESNKIDlkILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPN 219
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 767992314 1044 AFNLRGQSPLH--ILGQYGkenaaAIFDLFLECMP 1076
Cdd:PHA03100  220 LVNKYGDTPLHiaILNNNK-----EIFKLLLNNGP 249
FYVE_WDFY1 cd15756
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ...
1145-1206 5.41e-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: 5.41e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767992314 1145 PPWCDGSYCYECTARF-----------GVTTRKHHCRHCGRLLCHKCSTKE--IPIIKFDLNkpVRVCNICFDVL 1206
Cdd:cd15756     1 PQWLESDSCQKCEQPFfwnikqmwdtkTLGLRQHHCRKCGQAVCGKCSSKRssYPIMGFEFQ--VRVCDSCFETI 73
Ank_2 pfam12796
Ankyrin repeats (3 copies);
986-1065 5.63e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 5.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   986 LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAeafNLRGQSPLHILGQYGKENAA 1065
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
PHA02878 PHA02878
ankyrin repeat protein; Provisional
588-868 6.17e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 6.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  588 PLHMAIAYNHPDVVSVILEQKANA----------LH----ATNNLQIIPDFSLKDSRDQTVLGLALWTGMHT----IAAQ 649
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVnqpdhrdltpLHiickEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNrnveIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  650 LLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDE 729
Cdd:PHA02878  120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  730 KGNPPLWLALANNLEDIASTLVRHGCDATCwgpgPGGCLQTLLHRAIDE-NNEPTACFLIRSGCDVNSprqpgangegeE 808
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDA----RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNA-----------K 264
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992314  809 EARDGQTPLHLAASwgLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV-IIQLLVSH 868
Cdd:PHA02878  265 SYILGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCInIGRILISN 323
FYVE2_Vac1p_like cd15737
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ...
1146-1202 8.55e-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: 59.44  E-value: 8.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314 1146 PWCDGS---YCYECTARFGVTTRKHHCRHCGRLLCH----KCSTkEIPI--------------IKFDLNKP-----VRVC 1199
Cdd:cd15737     1 PWEDDSsvtHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCST-EVPLdllssalpdlpfvfKEPQSDIPddtksVRVC 79

                  ...
gi 767992314 1200 NIC 1202
Cdd:cd15737    80 RDC 82
BTB_POZ_BTBD9 cd18287
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
100-192 8.60e-11

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: 60.33  E-value: 8.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  100 VADLYEQEQYSDLKIKVGDRHISAHKFVLAARSdSWSLANL------SSTKELDLSDANPEVTMTMLRWIYTDELEFR-- 171
Cdd:cd18287    13 IGALFLNEEYSDVTFVVEEKRFPAHRVILAARS-EYFRALLyggmreSQQSEIELKDTNAEAFKALLKYIYTGRLTLTdl 91
                          90       100
                  ....*....|....*....|.
gi 767992314  172 EDDVFLtELMKLANRFQLQLL 192
Cdd:cd18287    92 KEDVLL-DVLGLAHQYGFEEL 111
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
769-887 9.09e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 66.19  E-value: 9.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  769 QTLLHRAIDENNEPTACFLIRSGCDVNSPRqpgANGEGEEEARD-----GQTPLHLAASWGLEETVQCLLEFGANVNAQD 843
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVSPR---ATGTFFRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767992314  844 AEGRTPIHVAISSQHGV----IIQLLVSHpDIHLN------VRDRQGLTPFACA 887
Cdd:cd22192   167 SLGNTVLHILVLQPNKTfacqMYDLILSY-DKEDDlqpldlVPNNQGLTPFKLA 219
PHA02876 PHA02876
ankyrin repeat protein; Provisional
391-756 9.61e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 9.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  391 IAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQlDLELKDHEGSTALWLAVQHITVSSDQSVnpfedvpV 470
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA-DVNIIALDDLSVLECAVDSKNIDTIKAI-------I 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  471 VNGTSFDENSFAarLIQRGSHTDAPDTatgncllqraagagneaaaLFLATNGAHVNHRNKWGETPLHTACRH-GLANLT 549
Cdd:PHA02876  232 DNRSNINKNDLS--LLKAIRNEDLETS-------------------LLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLV 290
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  550 AELLQQGANPNLQ-----------------TEEALPLPKEAASLTSlADSVHLqTPLHMAIAYN-HPDVVSVILEQKANA 611
Cdd:PHA02876  291 PKLLERGADVNAKnikgetplylmakngydTENIRTLIMLGADVNA-ADRLYI-TPLHQASTLDrNKDIVITLLELGANV 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  612 lhatnnlqiipdfSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDS-KSALFLLEHQADI 690
Cdd:PHA02876  369 -------------NARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANV 435
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314  691 NvSRTQDGETALQLAIRNQL-PLVVDAICTRGADMSVPDEKGNPPLWLALAnnLEDIASTLVRHGCD 756
Cdd:PHA02876  436 N-SKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNAINIQNQYPLLIALE--YHGIVNILLHYGAE 499
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
1153-1206 1.05e-10

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: 58.27  E-value: 1.05e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767992314 1153 CYECTARF-GVTTRKHHCRHCGRLLCHKCSTKEIPiIKFDLNKPVRVCNICFDVL 1206
Cdd:cd15741    12 CMRCKEPFnALTRRRHHCRACGYVVCWKCSDYKAT-LEYDGNKLNRVCKHCYVIL 65
PHA03100 PHA03100
ankyrin repeat protein; Provisional
254-432 1.71e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  254 KMIKSKTEYPLHKAIK-VEREDVVFLYLIemdSQLPGKLNEADHNGDLALDLALSRRLES--IATTLVSHKADVDMVDKS 330
Cdd:PHA03100   64 STKNNSTPLHYLSNIKyNLTDVKEIVKLL---LEYGANVNAPDNNGITPLLYAISKKSNSysIVEYLLDNGANVNIKNSD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  331 GWSLLH---KGIQRgDLFAATFLIKNGAFVNAAT-------LGAQ--------ETPLHLVALYSSKkhsadvmsemaQIA 392
Cdd:PHA03100  141 GENLLHlylESNKI-DLKILKLLIDKGVDINAKNrvnyllsYGVPinikdvygFTPLHYAVYNNNP-----------EFV 208
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767992314  393 EALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCK 432
Cdd:PHA03100  209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
BTB_POZ_KLHL7 cd18237
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
103-210 3.13e-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: 59.04  E-value: 3.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  103 LYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSL---ANL--SSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVfl 177
Cdd:cd18237    15 MRKQKTLCDVILIVEGREIKAHRVVLAAASHFFHLmftSNMteSKSSEVELKDAEPDIIELLVEFAYTARISVNSNNV-- 92
                          90       100       110
                  ....*....|....*....|....*....|...
gi 767992314  178 TELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18237    93 QSLLDAANQYQIEPVKKMCVDFLKEQLDASNCL 125
PHA02875 PHA02875
ankyrin repeat protein; Provisional
811-941 3.37e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.86  E-value: 3.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  811 RDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIhLNVRDRQGLTPFACAMTF 890
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAK 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767992314  891 KNNKSAEAILkrESGAaeQVDNKGRN----FLHVAVQNSDIESVLFLISVHANVN 941
Cdd:PHA02875  179 GDIAICKMLL--DSGA--NIDYFGKNgcvaALCYAIENNKIDIVRLFIKRGADCN 229
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
1151-1204 3.43e-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: 56.75  E-value: 3.43e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767992314 1151 SYCYECTA-RFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNkPVRVCNICFD 1204
Cdd:cd15724     8 SVCMVCQVeRFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYREN-PVRVCDQCYE 61
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
1149-1206 3.54e-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: 57.34  E-value: 3.54e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767992314 1149 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlnKPVRVCNICFDVL 1206
Cdd:cd15759     9 EATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSP--KPVRVCDSCHAML 64
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
812-874 4.12e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.15  E-value: 4.12e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767992314  812 DGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIHLN 874
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
BTB_POZ_SPOPL cd18343
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
95-208 5.20e-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: 5.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   95 RLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSL-----ANLSSTKELDLSDANPEVTMTMLRWIYTDE-- 167
Cdd:cd18343     7 RLAEDLGNLWENSRFTDCSLFVGGQEFKAHKSILAARSPVFNAmfeheMEESKKNRVEINDVDPEVFKEMMRFIYTGKap 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767992314  168 -LEFREDDvflteLMKLANRFQLQLLRERCEKGVMSLVNVRN 208
Cdd:cd18343    87 nLDKMADN-----LLAAADKYALERLKVMCEEALCNNLSVEN 123
BTB_POZ_roadkill-like cd18345
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
103-208 6.62e-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: 6.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  103 LYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIYTDE---LEFREDD 174
Cdd:cd18345    12 LFERSAFSDVTLCVGGREFQAHKAILAARSPVFNAMFEHEMEErkqnrVEITDVDHEVMREMLRFIYTGKapnLDKMADD 91
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767992314  175 vflteLMKLANRFQLQLLRERCEKGVMSLVNVRN 208
Cdd:cd18345    92 -----LLAAADKYALERLKVMCEEALCSNLSVEN 120
Ank_2 pfam12796
Ankyrin repeats (3 copies);
635-728 7.91e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 7.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   635 LGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHqadINVSRTQDGETALQLAIRNQLPLVV 714
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 767992314   715 DAICTRGADMSVPD 728
Cdd:pfam12796   78 KLLLEKGADINVKD 91
BTB2_POZ_BTBD8 cd18286
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
103-194 1.07e-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: 57.27  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  103 LYEQEQYSDLKIKVGDRHISAHKFVLAARS--------DSWSlanLSSTKELDLSDANPEVTMTMLRWIYTDELEFrEDD 174
Cdd:cd18286    11 LFLNGEDSDITIKVDGKTFKAHRCILCARSsyfaamlsGSWA---ESNSSEITLTGVSHAAVSFVLLFIYGGVLDL-PDD 86
                          90       100
                  ....*....|....*....|
gi 767992314  175 VFLTELMKLANRFQLQLLRE 194
Cdd:cd18286    87 VNLGELLSLADMYGLDGLKD 106
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
1153-1203 1.12e-09

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: 55.71  E-value: 1.12e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767992314 1153 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPiIKFDLNKPVRVCNICF 1203
Cdd:cd15742    12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYP-LKYLKDRPAKVCDGCF 61
BTB_POZ_RCBTB1_2 cd18298
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
110-198 1.18e-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: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  110 SDLKIKVGDRHISAHKFVLAARSD--SWSLANLSSTKELD---LSDANPEVTMTMLRWIYTDELEFREDDVFltELMKLA 184
Cdd:cd18298    13 SDLKFRVDGKYIYVHKAILKIRCEyfRSMFQSHWNEDDKNvieIDQYSYPVYYAFLRYLYTDQVDLPPEDAI--GLLDLA 90
                          90
                  ....*....|....
gi 767992314  185 NRFQLQLLRERCEK 198
Cdd:cd18298    91 NSYCEERLKKLCED 104
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
1153-1203 1.35e-09

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: 54.82  E-value: 1.35e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767992314 1153 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1203
Cdd:cd15745     2 CAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVPDTCIYLRVCKTCY 52
PHA03100 PHA03100
ankyrin repeat protein; Provisional
535-757 1.56e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  535 TPLHTACRHGLANLTAELLQQGANPNLQTE-EALPLPKEAasltsladsvhlqtpLHMAIAYNHPDVVSVILEQKANaLH 613
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKnNSTPLHYLS---------------NIKYNLTDVKEIVKLLLEYGAN-VN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  614 ATNNLQIIPDFSLKDSRDQTVlglalwtgmhTIAAQLLGSGAAINDTMSDGQTLLHMAIQ--RQDSKSALFLLEHQADIN 691
Cdd:PHA03100  101 APDNNGITPLLYAISKKSNSY----------SIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDIN 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  692 V---------------SRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCD 756
Cdd:PHA03100  171 AknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250

                  .
gi 767992314  757 A 757
Cdd:PHA03100  251 I 251
PHA02874 PHA02874
ankyrin repeat protein; Provisional
518-756 2.30e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  518 FLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLqteeaLPLPK-EAASLTSLADS--------VHLQTP 588
Cdd:PHA02874   53 LFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI-----LPIPCiEKDMIKTILDCgidvnikdAELKTF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  589 LHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLL 668
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGA-------------DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  669 HMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAI---RNQLPLVVDaictrGADMSVPDEKGNPPLWLALANNLE- 744
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHIMN-KCKNGFTPLHNAIihnRSAIELLIN-----NASINDQDIDGSTPLHHAINPPCDi 268
                         250
                  ....*....|..
gi 767992314  745 DIASTLVRHGCD 756
Cdd:PHA02874  269 DIIDILLYHKAD 280
PHA03100 PHA03100
ankyrin repeat protein; Provisional
943-1121 2.33e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  943 RVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQ-----DLPTICSVLLENGVDFAAVDENGNN 1017
Cdd:PHA03100   29 DYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGIT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314 1018 ALHLAVMHgRLNNIRV--LLTECTVDAEAFNLRGQSPLHILGQYGKE---------------NAAAIFDLFLECmpGYPL 1080
Cdd:PHA03100  109 PLLYAISK-KSNSYSIveYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdiNAKNRVNYLLSY--GVPI 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767992314 1081 DKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGV 1121
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 ...
102-210 2.39e-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: 56.77  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  102 DLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW-----SLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 176
Cdd:cd18340    20 DLLDHNKFVDCVLKIKEKEFPCHRLVLAACSPYFramflSDLEESKKREIVLEDVDPDVMGKILHYIYTSEIEITEQNV- 98
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767992314  177 lTELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18340    99 -QDIFAAANMFQIPSIFTVCVSFLQKRLCLSNCL 131
BTB1_POZ_RhoBTB cd18299
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
102-197 2.51e-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: 55.68  E-value: 2.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  102 DLYEQEQYSDLKIKVGDRH-ISAHKFVLAARSDSWSLANLSSTK-ELDlSDANPEVTMTMLRWIYTDELEFREDDvfLTE 179
Cdd:cd18299     5 NLLHSPSCADVVFILQGGVrIFAHRIVLAAASSVFADLFLMMTVvTLD-SDITPEAFRRVLEFLYTGVLDENEDD--LKE 81
                          90
                  ....*....|....*...
gi 767992314  180 LMKLANRFQLQLLRERCE 197
Cdd:cd18299    82 LKDAAELLELFDLVMMCT 99
PHA03095 PHA03095
ankyrin-like protein; Provisional
522-873 5.73e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 5.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  522 NGAHVNHRNKWGETPLHTACRHGLANLTAE---LLQQGANPNlqteealplpkeAASLTSLadsvhlqTPLHMAIAYNhp 598
Cdd:PHA03095   36 AGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVN------------APERCGF-------TPLHLYLYNA-- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  599 DVVSVIleqkanalhatnnlqiipDFslkdsrdqtvlglalwtgmhtiaaqLLGSGAAINDTMSDGQTLLH--MAIQRQD 676
Cdd:PHA03095   95 TTLDVI------------------KL-------------------------LIKAGADVNAKDKVGRTPLHvyLSGFNIN 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  677 SKSALFLLEHQADINvSRTQDGETALQLAIRNQ------LPLVVDAictrGADMSVPDEKGNPPLWlALANNL---EDIA 747
Cdd:PHA03095  132 PKVIRLLLRKGADVN-ALDLYGMTPLAVLLKSRnanvelLRLLIDA----GADVYAVDDRFRSLLH-HHLQSFkprARIV 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  748 STLVRHGCDATcwgpGPGGCLQTLLHRAidenNEPTAC------FLIRSGCDVNsprqpgangegeEEARDGQTPLHLAA 821
Cdd:PHA03095  206 RELIRAGCDPA----ATDMLGNTPLHSM----ATGSSCkrslvlPLLIAGISIN------------ARNRYGQTPLHYAA 265
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767992314  822 SWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQL-LVSHPDIHL 873
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 ...
95-208 6.06e-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: 6.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   95 RLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIYTDE-- 167
Cdd:cd18279     4 RLAEDLGNLWENSRFTDCCLCVGGQEFQAHKAILAARSPVFSAMFEHEMEEskknrVEINDVDPEVFKEMMRFIYTGKap 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767992314  168 -LEFREDDvflteLMKLANRFQLQLLRERCEKGVMSLVNVRN 208
Cdd:cd18279    84 nLDKMADD-----LLAAADKYALERLKVMCEDALCSNLSVEN 120
BTB_POZ_BTBD17 cd18292
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
89-198 6.30e-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: 54.98  E-value: 6.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   89 SESFISRLlaivADLYEQEQYSDLKIKVGDRHISAHKFVLAARSD--------SWSLANLSSTKELDLSDANPEVTMTML 160
Cdd:cd18292     1 SREFLQDI----AQLYNNEELSDIVLRVGGKVFHAHRLILAKSSDvfrvmlsnDWWSESKQSEIELVEDPECAAVFEKFL 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767992314  161 RWIYTDELEFREDDVFltELMKLANRFQLQLLRERCEK 198
Cdd:cd18292    77 RYLYTGQISVNLETAL--PLLMLADKYNVTDLKQLCVD 112
FYVE_WDFY2 cd15757
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ...
1145-1202 6.42e-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: 53.53  E-value: 6.42e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992314 1145 PPWCDGSYCYECTARF-----------GVTTRKHHCRHCGRLLCHKCSTKE--IPIIKFDLNkpVRVCNIC 1202
Cdd:cd15757     1 PEWLDSDSCQKCDQPFfwnfkqmwdskKIGLRQHHCRKCGKAVCGKCSSKRstIPLMGFEFE--VRVCDSC 69
PHA02874 PHA02874
ankyrin repeat protein; Provisional
523-739 8.20e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 8.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  523 GAHVNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVS 602
Cdd:PHA02874  114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG-------------------CYPIHIAIKHNFFDIIK 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  603 VILEQKANAlhatnnlqiipdfSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRqdSKSALF 682
Cdd:PHA02874  175 LLLEKGAYA-------------NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH--NRSAIE 239
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  683 LLEHQADINVSRTqDGETALQLAIrnQLPL---VVDAICTRGADMSVPDEKGNPPLWLAL 739
Cdd:PHA02874  240 LLINNASINDQDI-DGSTPLHHAI--NPPCdidIIDILLYHKADISIKDNKGENPIDTAF 296
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
1153-1203 8.20e-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: 8.20e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767992314 1153 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlNKPVRVCNICF 1203
Cdd:cd15749     2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRKG-NQKQKVCKQCH 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
518-610 1.29e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.20  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   518 FLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQgANPNLQTEEalplpkeaasltsladsvhlQTPLHMAIAYNH 597
Cdd:pfam12796   15 LLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG--------------------RTALHYAARSGH 73
                           90
                   ....*....|...
gi 767992314   598 PDVVSVILEQKAN 610
Cdd:pfam12796   74 LEIVKLLLEKGAD 86
BTB_POZ_KLHL1-like cd18234
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
110-210 1.53e-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: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  110 SDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTK-----ELDLSDANPEVTMTMLRWIYTDELEFREDDVflTELMKLA 184
Cdd:cd18234     2 CDVILIAGDRRIPAHRLVLSAVSDYFAAMFTNDVReateeEIKLKDVDPDALWTLVQYCYTGRLELKEDNV--ESLLATA 79
                          90       100
                  ....*....|....*....|....*.
gi 767992314  185 NRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18234    80 CLLQLSEVVEACCGFLMKQLHPSNCL 105
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
1153-1203 1.84e-08

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: 51.80  E-value: 1.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767992314 1153 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPI---IKFDLN-KPVRVCNICF 1203
Cdd:cd15736     2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLnlsAYDPRNgKWYRCCHSCF 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
815-866 2.19e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 2.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767992314   815 TPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLV 866
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
702-796 2.48e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 2.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   702 LQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHgCDATCWGPGpggclQTLLHRAIDENNE 781
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-----RTALHYAARSGHL 74
                           90
                   ....*....|....*
gi 767992314   782 PTACFLIRSGCDVNS 796
Cdd:pfam12796   75 EIVKLLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
313-463 3.10e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  313 IATTLVSHKADVDMVDK-SGWSLLHKGIQRGDLFAATFLIKNGAFVNAATLGaQETPLHLVALYSSKKhsadvmsemaqI 391
Cdd:PHA02878  149 ITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKT-NNSPLHHAVKHYNKP-----------I 216
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767992314  392 AEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLDLELKdhegSTALWLAVQHITVSSDQSVN 463
Cdd:PHA02878  217 VHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAK----SYILGLTALHSSIKSERKLK 284
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
1155-1203 3.20e-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: 51.17  E-value: 3.20e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 767992314 1155 ECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 1203
Cdd:cd15738    13 SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGHLSQRPVPVCRACY 61
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
813-940 3.54e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 3.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  813 GQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLL-----VSHPDIHLNVrdrqgltpfACA 887
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasISDPHAAGDL---------LCT 628
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767992314  888 MTFKNNKSAEAILKRESGAAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANV 940
Cdd:PLN03192  629 AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
384-453 3.55e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 3.55e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   384 VMSEMAQIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLDLelkDHEGSTALWLAVQH 453
Cdd:pfam12796    5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARS 71
BTB_POZ_KLHL8 cd18238
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
102-210 3.61e-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: 53.06  E-value: 3.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  102 DLYEQEQYSDLKIKVGDRHISAHKFVLAARSD---SWSLANLSSTKE--LDLSDANPEVTMTMLRWIYTDELEFREDDVf 176
Cdd:cd18238     8 QFYENGELCDVTLKVGEKSIHCHRLVLACVSPyfrAMFTSEMAESKQdsITIKDIDEEAVELLVDFAYTGKLTLTVDNV- 86
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767992314  177 lTELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18238    87 -QSLLYAASLLQVEEVAKACCEFMKDHLHPSNCL 119
BTB_POZ_BPM_plant cd18280
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
101-197 3.81e-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: 3.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  101 ADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW------SLANlSSTKELDLSDANPEVTMTMLRWIYTDEL------ 168
Cdd:cd18280     6 GALLESEEGADVTFNVDGEKFRAHKLVLAARSPVFrsmlfgPMRE-ENEGEIVIEDVEPPVFKALLHFIYKDELpddvep 84
                          90       100       110
                  ....*....|....*....|....*....|...
gi 767992314  169 ----EFREDDVFLTELMKLANRFQLQLLRERCE 197
Cdd:cd18280    85 agsdSSSLDTTMAQHLLAAADRYALERLRLLCE 117
BTB_POZ_KBTBD3_BKLHD3 cd18271
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
89-211 4.70e-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: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   89 SESFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELD-----LSDANPEVTMTMLRWI 163
Cdd:cd18271     4 AECHGQQILSVLQNFREQNAFFDFNIIVKDETIPCHRCVLAACSDFFRAMFEVNMKERDdgsvtISNLSPKAVKAFLDYA 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767992314  164 YTDELEFREDDVFLteLMKLANRFQLQLLRERCEKGVMSLVNVRNCIR 211
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 ...
102-189 5.02e-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: 5.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  102 DLYEQEQYSDLKIKVGDRHISAHKFVLAA-----RSDSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 176
Cdd:cd18269    20 DLLDENKFVDCVLKIGDKEFPCHRLVLAAcspyfRAMFLSDLEESKKKEVVLEDVDPDVMGMILKYLYTSEIDLNDQNV- 98
                          90
                  ....*....|...
gi 767992314  177 lTELMKLANRFQL 189
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 ...
94-210 5.17e-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: 52.79  E-value: 5.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   94 SRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSL-----ANLSSTKELDLSDANPEVTMTMLRWIYTDEL 168
Cdd:cd18256     5 SLILAQLNKLRGQHEFCDVQLQVGMELFSVHRLVLAASSPYFAAlfaggMSESSKDVVQIHGVEPDIFHILLDFIYTGVV 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767992314  169 EFREDDVflTELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18256    85 EVTVSNV--QELLVAADMLQLTEVVEICCEFLKGQLHPSNCI 124
PHA02874 PHA02874
ankyrin repeat protein; Provisional
339-672 5.22e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 5.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  339 IQRGDLFAATFLIKNGAFVN------------AATLGAQETPLHLV--ALYSSKKHSADVMSEMAQiaeALLQAGANPNM 404
Cdd:PHA02874   43 IRSGDAKIVELFIKHGADINhintkiphplltAIKIGAHDIIKLLIdnGVDTSILPIPCIEKDMIK---TILDCGIDVNI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  405 QDSKGRTPLHVSIMAGNEYVFSQLLQCKQlDLELKDHEGSTALWLAVQHitvssdqsvNPFEDVPVvngtsfdensfaar 484
Cdd:PHA02874  120 KDAELKTFLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKH---------NFFDIIKL-------------- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  485 LIQRGSHTDAPDTaTGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRHGLAnlTAELLQQGANPNLQte 564
Cdd:PHA02874  176 LLEKGAYANVKDN-NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS--AIELLINNASINDQ-- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  565 ealplpkeaasltsladSVHLQTPLHMAIayNHP---DVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLGLAL-W 640
Cdd:PHA02874  251 -----------------DIDGSTPLHHAI--NPPcdiDIIDILLYHKA-------------DISIKDNKGENPIDTAFkY 298
                         330       340       350
                  ....*....|....*....|....*....|....
gi 767992314  641 TGMHTIAAQLLGSGAAIN--DTMSDGQTLLHMAI 672
Cdd:PHA02874  299 INKDPVIKDIIANAVLIKeaDKLKDSDFLEHIEI 332
Ank_2 pfam12796
Ankyrin repeats (3 copies);
772-843 5.85e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 5.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   772 LHRAIDENNEPTACFLIRSGCDVNSPRQPG-------ANGEGEEEAR------------DGQTPLHLAASWGLEETVQCL 832
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGrtalhlaAKNGHLEIVKlllehadvnlkdNGRTALHYAARSGHLEIVKLL 80
                           90
                   ....*....|.
gi 767992314   833 LEFGANVNAQD 843
Cdd:pfam12796   81 LEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
334-714 1.07e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  334 LLHKGIQRGDLFAATFLIKNGAFVNAATLGAQeTPLHLVALYSSkkhsadvmsemAQIAEALLQAGANPNMQDSKGRTPL 413
Cdd:PHA02876  148 LIKERIQQDELLIAEMLLEGGADVNAKDIYCI-TPIHYAAERGN-----------AKMVNLLLSYGADVNIIALDDLSVL 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  414 HVSIMAGN----EYVFSQLLQCKQLDLEL----KDHEGSTALWLAVQHITVSsdqSVNPFEDVPVVNGTSFDENS-FAAR 484
Cdd:PHA02876  216 ECAVDSKNidtiKAIIDNRSNINKNDLSLlkaiRNEDLETSLLLYDAGFSVN---SIDDCKNTPLHHASQAPSLSrLVPK 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  485 LIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACR-HGLANLTAELLQQGANPNlqt 563
Cdd:PHA02876  293 LLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVN--- 369
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  564 eealplpkeaasltslADSVHLQTPLHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLGLALW-TG 642
Cdd:PHA02876  370 ----------------ARDYCDKTPIHYAAVRNNVVIINTLLDYGA-------------DIEALSQKIGTALHFALCgTN 420
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767992314  643 MHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSAL-FLLEHQADINVsrtqdgetalqLAIRNQLPLVV 714
Cdd:PHA02876  421 PYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIeMLLDNGADVNA-----------INIQNQYPLLI 482
PHA03095 PHA03095
ankyrin-like protein; Provisional
350-758 1.30e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  350 LIKNGAFVN-AATLGaqETPLHLVALYSSKKhsadvmseMAQIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQL 428
Cdd:PHA03095   33 LLAAGADVNfRGEYG--KTPLHLYLHYSSEK--------VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  429 LQCKQLDLELKDHEGSTALwlavqHITVSsdqsvNPFEDVPVVNgtsfdensfaarliqrgshtdapdtatgncllqraa 508
Cdd:PHA03095  103 LIKAGADVNAKDKVGRTPL-----HVYLS-----GFNINPKVIR------------------------------------ 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  509 gagneaaalFLATNGAHVNHRNKWGETPLHTACRHglANLTAELLqqganpNLqteealpLPKEAASLTslADSVHLQTP 588
Cdd:PHA03095  137 ---------LLLRKGADVNALDLYGMTPLAVLLKS--RNANVELL------RL-------LIDAGADVY--AVDDRFRSL 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  589 LHMAIAYNHPD--VVSVILEQKANALhATNNLQIIPDFSLKdsrdqtvlglALWTGMHTIAAQLLGSGAAINDTMSDGQT 666
Cdd:PHA03095  191 LHHHLQSFKPRarIVRELIRAGCDPA-ATDMLGNTPLHSMA----------TGSSCKRSLVLPLLIAGISINARNRYGQT 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  667 LLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAIRNQlplvvDAICTRGAdmsvpdEKGNPPLwLALANNLEDI 746
Cdd:PHA03095  260 PLHYAAVFNNPRACRRLIALGADINA-VSSDGNTPLSLMVRNN-----NGRAVRAA------LAKNPSA-ETVAATLNTA 326
                         410
                  ....*....|..
gi 767992314  747 ASTLVRHGCDAT 758
Cdd:PHA03095  327 SVAGGDIPSDAT 338
PHA02875 PHA02875
ankyrin repeat protein; Provisional
296-451 1.41e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  296 HNGDLALDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNAATLGAQETPLHLvaly 375
Cdd:PHA02875   33 YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHL---- 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767992314  376 SSKKHSADVMsemaqiaEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLdLELKDHEGSTALWLAV 451
Cdd:PHA02875  109 ATILKKLDIM-------KLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAM 176
PHA02878 PHA02878
ankyrin repeat protein; Provisional
768-970 1.53e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  768 LQTLLHRAIDENNEPTACFLIRSGCDVNSPRqpgangegeeeaRDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGR 847
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANVNIPD------------KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  848 TPIHVAISSQHGV-IIQLLVSHpDIHLNVRDR-QGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHVAVQNS 925
Cdd:PHA02878  236 TPLHISVGYCKDYdILKLLLEH-GVDVNAKSYiLGLTA----------------------------------LHSSIKSE 280
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767992314  926 DIESVLflISVHANVNSrvQDASKLTPLHLAVQAGSEIIVRNLLL 970
Cdd:PHA02878  281 RKLKLL--LEYGADINS--LNSYKLTPLSSAVKQYLCINIGRILI 321
BTB_POZ_KBTBD4 cd18272
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
94-211 1.66e-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: 51.82  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   94 SRLLAIVADL-YEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIYTDE 167
Cdd:cd18272    16 SRVAQSIMDLcLEDGLFADVTISVEGKEFQLHRLVLSAQSCFFRSMFTSNLKEarnrvIELKDVSESVFQLLVDYIYHGT 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767992314  168 LEFREDDvfLTELMKLANRFQLQLLRERCEKGVMSLVNVRNCIR 211
Cdd:cd18272    96 VKLRVEE--LQETYEVADMYQLTALFEECSRFLARTVQVRNCLQ 137
PHA02875 PHA02875
ankyrin repeat protein; Provisional
918-1111 1.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  918 LHVAVQNSDIESVLFLISVHANVNSRVQDASklTPLHLAVQAGSEIIVRNLLLAGAKVNELT-KHRQTALHLAAQQDLPT 996
Cdd:PHA02875   39 IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE--SELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  997 ICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtectvdaeafnlrgqsplhilgqygKENAAaifdlflecmp 1076
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI-------------------------DHKAC----------- 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 767992314 1077 gypLDKPDADGSTVLLLAYMKGNANLCRAIVRSGA 1111
Cdd:PHA02875  161 ---LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
1149-1203 1.79e-07

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: 49.10  E-value: 1.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767992314 1149 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCStkEIPIIKFDLNKPVRVCNICF 1203
Cdd:cd15726     6 DVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACS--NFYVLTAHGGKKERCCKACF 58
PHA03098 PHA03098
kelch-like protein; Provisional
114-281 2.76e-07

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 54.77  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  114 IKVGDRHISAHKFVLAARSDSWS--LANLSSTKELDLSDaNPEVTMTMLRWIYTDELEFREDDVflTELMKLANRFQLQL 191
Cdd:PHA03098   16 IVNGGGIIKVHKIILSSSSEYFKkmFKNNFKENEINLNI-DYDSFNEVIKYIYTGKINITSNNV--KDILSIANYLIIDF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  192 LRERCEKGVMSLVNVRNCIRFYQTAEELNASTLMNYCAEIIASHWDDLRK-EDFSSMSAQLLYKMIKSKTeyplhkaIKV 270
Cdd:PHA03098   93 LINLCINYIIKIIDDNNCIDIYRFSFFYGCKKLYSAAYNYIRNNIELIYNdPDFIYLSKNELIKILSDDK-------LNV 165
                         170
                  ....*....|.
gi 767992314  271 EREDVVFLYLI 281
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 ...
82-196 3.63e-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: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   82 QANKESSSESFisrllaivADLYEQEQYSDLKIKVGD----------RHISAHKFVLAARS---DSWSLANLSSTK-ELD 147
Cdd:cd18346     3 QATKSSLKERF--------AFLFNNELLSDVRFVVGKgrprgpgpgaQRIPAHRFVLAAGSavfDAMFNGGMATTSaEIE 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767992314  148 LSDANPEVTMTMLRWIYTDELEFREDDVFLTelMKLANRFQLQLLRERC 196
Cdd:cd18346    75 LPDVEPAAFLALLRFLYSDEVQIGPETVMTT--LYTAKKYAVPALEAHC 121
PHA02878 PHA02878
ankyrin repeat protein; Provisional
391-674 3.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  391 IAEALLQAGANPNMQDSKGRTPLHVSIMAGN----EYVFSQLLQCKQLDLELKDHEGSTALWLAVQHITVSSDQSVNPFE 466
Cdd:PHA02878   52 VVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTI 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  467 DVPVVNGTSFD---ENSFAARLIQRGSHTDAPDTATGNCLLQRAAGAGNEAAALFLATNGAHVNHRNKWGETPLHTACRH 543
Cdd:PHA02878  132 DLVYIDKKSKDdiiEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  544 GLANLTAELLQQGANPNlqteealplpkeaasltslADSVHLQTPLHMAIAY-NHPDVVSVILEQKA--NALHATNNLQI 620
Cdd:PHA02878  212 YNKPIVHILLENGASTD-------------------ARDKCGNTPLHISVGYcKDYDILKLLLEHGVdvNAKSYILGLTA 272
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767992314  621 IpDFSLKDSRdqtVLGLalwtgmhtiaaqLLGSGAAINDTMSDGQTLLHMAIQR 674
Cdd:PHA02878  273 L-HSSIKSER---KLKL------------LLEYGADINSLNSYKLTPLSSAVKQ 310
PHA03100 PHA03100
ankyrin repeat protein; Provisional
519-692 3.86e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  519 LATNGAHVNHRNKWGETPLHTACRHGLANLT--AELLQQGANPNLQTEEALPLpkeaasltsladsvhlqtpLHMAIAYN 596
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKKSNSYSivEYLLDNGANVNIKNSDGENL-------------------LHLYLESN 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  597 HPD--VVSVILEQKANaLHATNNLQII----PDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHM 670
Cdd:PHA03100  153 KIDlkILKLLIDKGVD-INAKNRVNYLlsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
                         170       180
                  ....*....|....*....|..
gi 767992314  671 AIQRQDSKSALFLLEHQADINV 692
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 ...
102-210 4.50e-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: 50.23  E-value: 4.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  102 DLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSS-----TKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 176
Cdd:cd18341    20 ELLDENKFVDCTLKAGDKSLPCHRLILAACSPYFREYFLSEeseekKKEVVLDNVDPNIMDMILKYLYSAEIDLNDGNV- 98
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767992314  177 lTELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18341    99 -QDIFALASRFQIPSVFTVCVTYLQKRLSPANCL 131
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
605-753 7.26e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  605 LEQKANALHATNNLQIIPDFSL--KDSRDQTVLglalwtgmHTIAA---QLLGSGaaindtmsdgqtllhmaiqrqDSKS 679
Cdd:PTZ00322   47 IDTHLEALEATENKDATPDHNLttEEVIDPVVA--------HMLTVelcQLAASG---------------------DAVG 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767992314  680 ALFLLEHQADINvSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRH 753
Cdd:PTZ00322   98 ARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
389-530 8.80e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  389 AQIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQcKQLDLELKDHEGSTALW--LAVQH-----ITVSSDQS 461
Cdd:PLN03192  538 AALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLK-HACNVHIRDANGNTALWnaISAKHhkifrILYHFASI 616
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767992314  462 VNPFedvpvvngTSFDENSFAAR---------LIQRGSHTDAPDTaTGNCLLQRAAGAGNEAAALFLATNGAHVNHRN 530
Cdd:PLN03192  617 SDPH--------AAGDLLCTAAKrndltamkeLLKQGLNVDSEDH-QGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_2 pfam12796
Ankyrin repeats (3 copies);
302-406 8.99e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 8.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   302 LDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLIKNgAFVNAATLGaqETPLHLVALYSSKKhs 381
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG--RTALHYAARSGHLE-- 75
                           90       100
                   ....*....|....*....|....*
gi 767992314   382 advmsemaqIAEALLQAGANPNMQD 406
Cdd:pfam12796   76 ---------IVKLLLEKGADINVKD 91
BTB_POZ_NS1BP cd18306
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
92-210 1.38e-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: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   92 FISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSdSWSLANLSSTKE------LDLSDANPEVTMTMLRWIYT 165
Cdd:cd18306     1 HPESVLAKLNALRKNRQFCDVILQVGGHEIPAHRAVLACAS-PYLFELFSSDSDgesiltVKLDGLDPDAVEVLVNYAYT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767992314  166 DELEFREDDVFltELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
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 ...
98-197 1.42e-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: 48.42  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   98 AIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW-SLANL----SSTKELDLSDANPEVTMTMLRWIYT---DELE 169
Cdd:cd18297     1 RIDPHYVNNPEMSDVTFLVEGRPFYAHKIVLVTASDRFkSMLSSgsteAQTPVIEIPDIRYDIFQLMMQYLYTggvESLD 80
                          90       100
                  ....*....|....*....|....*...
gi 767992314  170 FREDDVFltELMKLANRFQLQLLRERCE 197
Cdd:cd18297    81 VAQDDAL--ELLRAASFFQLDGLKRHCE 106
PHA02874 PHA02874
ankyrin repeat protein; Provisional
921-1060 1.75e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.89  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  921 AVQNSDIESVLFLISVHANVNSrvQDASKLTPLHLAVQAGSEIIVRNLLL-----------------------AGAKVNE 977
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINH--INTKIPHPLLTAIKIGAHDIIKLLIDngvdtsilpipciekdmiktildCGIDVNI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  978 LTKHRQTALHLAAQQ-DLPTIcSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPLHIL 1056
Cdd:PHA02874  120 KDAELKTFLHYAIKKgDLESI-KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EKGAYANVKDNNGESPLHNA 197

                  ....
gi 767992314 1057 GQYG 1060
Cdd:PHA02874  198 AEYG 201
BTB_POZ_KLHL18 cd18247
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
91-196 1.98e-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: 48.05  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   91 SFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW------SLANlSSTKELDLSDANPEVTMTMLRWIY 164
Cdd:cd18247     1 DLPSSGFPVMEEIRRQGKLCDVTLKVGDQKFSAHRIVLAATIPYFhamfthDMVE-SKQDEITMQGIEPSALEALINFAY 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767992314  165 TDELEFREDDVflTELMKLANRFQLQLLRERC 196
Cdd:cd18247    80 SGRIAIDTSNV--QSLLVGASFLQLQSVKDAC 109
Ank_4 pfam13637
Ankyrin repeats (many copies);
984-1035 2.42e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.42e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767992314   984 TALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLL 1035
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
824-1056 2.50e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 51.59  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  824 GLEET-VQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHpdihlnvrdrqGLTPFACAmtfKNNKSAEAILkr 902
Cdd:PHA02946   49 GLDERfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTH-----------GADPNACD---KQHKTPLYYL-- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  903 eSGAAEQVdnkgrnflhvavqnsdIESVLFLISVHANVNSRVqDASKLTPLhLAVQAGSEIIVRNLLLAGAKVNELTKHR 982
Cdd:PHA02946  113 -SGTDDEV----------------IERINLLVQYGAKINNSV-DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFG 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314  983 QTALHLAAQQDLPTICSV--LLENGVDFAAVDENGNNALHLaVMHGRLNNIRVL-LTECTVDAEAFNLRGQSPLHIL 1056
Cdd:PHA02946  174 KNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHI-VCSKTVKNVDIInLLLPSTDVNKQNKFGDSPLTLL 249
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
954-1044 2.79e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  954 HLAVqAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRV 1033
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                          90
                  ....*....|.
gi 767992314 1034 LLTECTVDAEA 1044
Cdd:PTZ00322  167 LSRHSQCHFEL 177
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
1153-1203 3.10e-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: 45.38  E-value: 3.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767992314 1153 CYECTARFG-VTTRKHHCRHCGRLLCHKCSTkeipiIKFDLNKPVRVCNICF 1203
Cdd:cd15740     8 CKGCNESFNsITKRRHHCKQCGAVICGKCSE-----FKDLASRHNRVCRDCF 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
769-958 3.39e-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: 51.42  E-value: 3.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  769 QTLLHRAIDENNEPTACFLIRSGCDVnsprQPGANGEGEEEARD-----GQTPLHLAASWGLEETVQCLLEFG---ANVN 840
Cdd:cd21882    74 QTALHIAIENRNLNLVRLLVENGADV----SARATGRFFRKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALE 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  841 AQDAEGRTPIHV--------------AISSQHGVIIQLLVSHPDIHLN-VRDRQGLTPFACAMTFKNNKSAEAILKRESG 905
Cdd:cd21882   150 AQDSLGNTVLHAlvlqadntpensafVCQMYNLLLSYGAHLDPTQQLEeIPNHQGLTPLKLAAVEGKIVMFQHILQREFS 229
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767992314  906 AAEQvdNKGRNF-------LHVA------VQNSDIESVLFLISVHANVNSRvQDASKLTPLHLAVQ 958
Cdd:cd21882   230 GPYQ--PLSRKFtewtygpVTSSlydlseIDSWEKNSVLELIAFSKKREAR-HQMLVQEPLNELLQ 292
BTB_POZ_KLHL1 cd18335
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
105-210 3.91e-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: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  105 EQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSST-----KELDLSDANPEVTMTMLRWIYTDELEFREDDVflTE 179
Cdd:cd18335    15 KQQQLCDVILIAGNRKIPAHRLVLSAVSDYFAAMFTSDVceakqEEIKMEGIDPNALWDLVQFAYTGCLELKEDTI--EN 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 767992314  180 LMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18335    93 LLAAACLLQLSQVVEVCCHFLMKLLHPSNCL 123
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
812-843 4.30e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.59  E-value: 4.30e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767992314   812 DGQTPLHLAA-SWGLEETVQCLLEFGANVNAQD 843
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
769-958 4.52e-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: 50.95  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  769 QTLLHRAIDENNEPTACFLIRSGCDVNSPR-----QPGANGEGeeeARDGQTPLHLAASWGLEETVQCLLEFG---ANVN 840
Cdd:cd22193    77 QTALHIAIERRQGDIVALLVENGADVHAHAkgrffQPKYQGEG---FYFGELPLSLAACTNQPDIVQYLLENEhqpADIE 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  841 AQDAEGRTPIH--VAIS-----------SQHGVIIQLLVS-HPDIHLN-VRDRQGLTPFACAMTFKNNKSAEAILKRE-- 903
Cdd:cd22193   154 AQDSRGNTVLHalVTVAdntkentkfvtRMYDMILIRGAKlCPTVELEeIRNNDGLTPLQLAAKMGKIEILKYILQREik 233
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767992314  904 SGAAEQVDNKGRNFLHVAVQNS--DI--------ESVLFLISVHANVNSRvQDASKLTPLHLAVQ 958
Cdd:cd22193   234 EPELRHLSRKFTDWAYGPVSSSlyDLsnvdtcekNSVLEIIVYNSKIDNR-HEMLTLEPLNTLLQ 297
BTB1_POZ_IBtk cd18301
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
111-166 5.47e-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: 46.13  E-value: 5.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767992314  111 DLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELDLSDANPEVTMT---------MLRWIYTD 166
Cdd:cd18301    20 DVVFQVGGKTFPAHKFILASRSDYFRKLFLSSLLTSEDAVGCDVVHIEkvppeifeqLLQFIYTD 84
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
518-724 5.61e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.64  E-value: 5.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  518 FLATNGAHvnHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNH 597
Cdd:PLN03192  512 LLGDNGGE--HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKG-------------------RTPLHIAASKGY 570
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  598 PDVVSVILEqkanalHATNnlqiipdFSLKDSRDQTVLGLALWTGMHTIaAQLLGSGAAINDTMSDGQtLLHMAIQRQDS 677
Cdd:PLN03192  571 EDCVLVLLK------HACN-------VHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHAAGD-LLCTAAKRNDL 635
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767992314  678 KSALFLLEHQADINvSRTQDGETALQLAIRNQLPLVVDAICTRGADM 724
Cdd:PLN03192  636 TAMKELLKQGLNVD-SEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
BTB_POZ_BTBD3_6 cd18282
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
103-178 5.83e-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: 5.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  103 LYEQEQYSDLKIKVGD----RHISAHKFVLAARSDSW------SLANlsSTKELDLSDANPEVTMTMLRWIYTDELEFRE 172
Cdd:cd18282     1 MFNNELMADVHFIVGPpggtQRIPAHKYVLATGSSVFyamfygGLAE--NKNEIEIPDVEPAAFLNLLRYLYCDEIDLEP 78

                  ....*.
gi 767992314  173 DDVFLT 178
Cdd:cd18282    79 DTVLAT 84
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
1153-1206 6.41e-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: 44.80  E-value: 6.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992314 1153 CYECTARFGV-TTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKP------VRVCNICFDVL 1206
Cdd:cd15723     2 CTGCGASFSVlLKKRRSCNNCGNAFCSRCCSKKVPRSVMGATAPaaqretVFVCSGCNDKL 62
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
1166-1203 7.31e-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: 44.33  E-value: 7.31e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 767992314 1166 KHHCRHCGRLLCHKCSTKEIPIIKFDLNkPVRVCNICF 1203
Cdd:cd15744    16 KHNCYNCGGTFCDACSSNELPLPSSIYE-PARVCDVCY 52
BTB_POZ_SPOP cd18342
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
95-208 7.73e-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: 7.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   95 RLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSL-----ANLSSTKELDLSDANPEVTMTMLRWIYTDELE 169
Cdd:cd18342     8 RLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAmfeheMEESKKNRVEINDVEPEVFKEMMCFIYTGKAP 87
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767992314  170 frEDDVFLTELMKLANRFQLQLLRERCEKGVMSLVNVRN 208
Cdd:cd18342    88 --NLDKMADDLLAAADKYALERLKVMCEDALCSNLSVEN 124
Ank_2 pfam12796
Ankyrin repeats (3 copies);
335-440 8.01e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 8.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   335 LHKGIQRGDLFAATFLIKNGAFVNAaTLGAQETPLHLVALYSSkkhsadvmsemAQIAEALLQaGANPNMQDsKGRTPLH 414
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGH-----------LEIVKLLLE-HADVNLKD-NGRTALH 66
                           90       100
                   ....*....|....*....|....*.
gi 767992314   415 VSIMAGNEYVFSQLLQCKQlDLELKD 440
Cdd:pfam12796   67 YAARSGHLEIVKLLLEKGA-DINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
299-609 8.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  299 DLALDLALSRrlESIATTLVSHKA--DVDMVDKSGWSLLHKGIQRGDLFA-ATFLIKNGAFVNAATLGAqETPLHLVA-- 373
Cdd:PHA02876  241 DLSLLKAIRN--EDLETSLLLYDAgfSVNSIDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKG-ETPLYLMAkn 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  374 ----------------------LYSSKKHSADVMSEMAQIAEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQC 431
Cdd:PHA02876  318 gydtenirtlimlgadvnaadrLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  432 KQlDLELKDHEGSTALWLAVqhitvssdQSVNPFEDVPVvngtsfdensfaarLIQRgshtdapdtatgncllqraagag 511
Cdd:PHA02876  398 GA-DIEALSQKIGTALHFAL--------CGTNPYMSVKT--------------LIDR----------------------- 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  512 neaaalflatnGAHVNHRNKWGETPLHTACRHGLA-NLTAELLQQGANPNlqteealplpkeaasltslADSVHLQTPLH 590
Cdd:PHA02876  432 -----------GANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVN-------------------AINIQNQYPLL 481
                         330
                  ....*....|....*....
gi 767992314  591 MAIAYNhpDVVSVILEQKA 609
Cdd:PHA02876  482 IALEYH--GIVNILLHYGA 498
BTB_POZ_KLHL4 cd18336
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
105-210 8.46e-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: 46.58  E-value: 8.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  105 EQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIYTDELEFREDDVflTE 179
Cdd:cd18336    15 QHKQLCDVLLIAGNLKIPAHRLVLSAVSDYFAAMFTNDVREakqeeIKMEGVDPDALKALVHYAYTGVLELKEDTI--ES 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 767992314  180 LMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18336    93 LLAAACLLQLSQVIDVCCNFLMKQLHPSNCL 123
PHA02946 PHA02946
ankyin-like protein; Provisional
808-988 8.68e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.67  E-value: 8.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  808 EEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVI--IQLLVSHPDIHLNVRDRQGLTP-F 884
Cdd:PHA02946   67 ETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKINNSVDEEGCGPlL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  885 ACamtfknNKSAEAILKRESG---AAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAV-QAG 960
Cdd:PHA02946  147 AC------TDPSERVFKKIMSigfEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCsKTV 220
                         170       180
                  ....*....|....*....|....*...
gi 767992314  961 SEIIVRNLLLAGAKVNELTKHRQTALHL 988
Cdd:PHA02946  221 KNVDIINLLLPSTDVNKQNKFGDSPLTL 248
PHA02874 PHA02874
ankyrin repeat protein; Provisional
256-453 1.04e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  256 IKSKTEYPLHKAIKVEREDVVFLYLIE-MDSQLpgkLNEADHNGDLAldlalsrrlesiaTTLVSHKADVDMVDKSGWSL 334
Cdd:PHA02874   64 INTKIPHPLLTAIKIGAHDIIKLLIDNgVDTSI---LPIPCIEKDMI-------------KTILDCGIDVNIKDAELKTF 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  335 LHKGIQRGDLFAATFLIKNGAFVNAATLGAQeTPLHLvalySSKKHSADvmsemaqIAEALLQAGANPNMQDSKGRTPLH 414
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGC-YPIHI----AIKHNFFD-------IIKLLLEKGAYANVKDNNGESPLH 195
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 767992314  415 VSIMAGnEYVFSQLLQCKQLDLELKDHEGSTALWLAVQH 453
Cdd:PHA02874  196 NAAEYG-DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH 233
BTB_POZ_KBTBD2_BKLHD1 cd18270
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
103-212 1.53e-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: 45.76  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  103 LYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWS---LANLSSTKE--LDLSDANPEVTMTMLRWIYTDELEFREDDVfl 177
Cdd:cd18270    20 FYEQQLLTDIVLIVEGTEFPCHKMVLATCSSYFRamfMSGLSESKQthVHLRNVDAATLQIIITYAYTGNLAINDSTV-- 97
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767992314  178 TELMKLANRFQLQLLRERCEKGVMSLVNVRNCIRF 212
Cdd:cd18270    98 EQLYETACFLQVEDVLQRCREYLIKKINAENCVRL 132
PHA02741 PHA02741
hypothetical protein; Provisional
813-894 1.56e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 46.57  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  813 GQTPLHLAA----SWGLEETVQCLLEFGANVNAQDA-EGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFACA 887
Cdd:PHA02741   60 GQMCIHIAAekheAQLAAEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139

                  ....*..
gi 767992314  888 MTFKNNK 894
Cdd:PHA02741  140 IDNEDVA 146
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
800-1005 1.57e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  800 PGANGeGEEEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPdIHLNVRDRQ 879
Cdd:PLN03192  513 LGDNG-GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDAN 590
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  880 GLTPFACAMTFKNNKSAEaILKRESGAAEQvdNKGRNFLHVAVQNSDIESVLFLISVHANVNSrvQDASKLTPLHLAVQA 959
Cdd:PLN03192  591 GNTALWNAISAKHHKIFR-ILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDS--EDHQGATALQVAMAE 665
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  960 GSEIIVRNLLLAGAKV--------------NELTKHRQTALHLAAQQDLPTICSVLLENG 1005
Cdd:PLN03192  666 DHVDMVRLLIMNGADVdkantdddfsptelRELLQKRELGHSITIVDSVPADEPDLGRDG 725
FYVE1_Vac1p_like cd15761
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ...
1150-1203 1.73e-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: 43.80  E-value: 1.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767992314 1150 GSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKeipIIKFDLNKPV--------RVCNICF 1203
Cdd:cd15761    10 KSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRN---RIKLNNSAEYdpkngkwcRCCEKCF 68
BTB_POZ_KBTBD8 cd18274
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
103-210 1.74e-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: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  103 LYEQEQYSDLKIKVG-DRHISAHKFVLAA-----RSDSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVf 176
Cdd:cd18274    16 MYDEGQLTDIVVEVDhGKTFSCHRNVLAAispyfRSMFTSGLTESTQKEVRIVGVEAESMHLVLDYAYTSRVTLTEANV- 94
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767992314  177 lTELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18274    95 -QALFTAASIFQIPSLQDQCAQFMISRLDPQNSI 127
BTB_POZ_BTBD1_2 cd18281
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
82-178 1.79e-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: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   82 QANKESSSESFisrllaivADLYEQEQYSDLKIKVG----DRHISAHKFVLAARS---DSWSLANLSSTK-ELDLSDANP 153
Cdd:cd18281     3 QASKTTVKERF--------AFLFNNETLSDVHFIVGkgdnEQRIPAHKFVLSIGSavfDAMFNGGMATTSaEIELPDVEP 74
                          90       100
                  ....*....|....*....|....*
gi 767992314  154 EVTMTMLRWIYTDELEFREDDVFLT 178
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 ...
92-198 2.58e-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: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   92 FISRLLaivadlyEQEQYSDLKIKVGDRHISAHKFVLAARSDSWslANLSSTK-----ELDLSDA--NPEVTMTMLRWIY 164
Cdd:cd18295     9 FLRRLL-------EQGSYSDVTFNVHGESFPAHRCILSARSPYF--AEMFETKwkdkrEINLKHPlvNPDAFRALLQYLY 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767992314  165 TDELEFREDDVflTELMKLANRFQLQLLRERCEK 198
Cdd:cd18295    80 TGRLEIHVDDV--EDCKRLAKQCRLEELIEELEA 111
PHA02859 PHA02859
ankyrin repeat protein; Provisional
923-1055 2.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.74  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  923 QNSDIESVLFLISVHANVNSRVQDaSKLTPLH--LAVQAGSEI-IVRNLLLAGAKVNELTKHRQTALHLAAqqdlpTICS 999
Cdd:PHA02859   62 DKVNVEILKFLIENGADVNFKTRD-NNLSALHhyLSFNKNVEPeILKILIDSGSSITEEDEDGKNLLHMYM-----CNFN 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767992314 1000 V-------LLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAEAFNLRGQSPLHI 1055
Cdd:PHA02859  136 VrinviklLIDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
BTB_POZ_KLHL5 cd18337
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
106-210 2.73e-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: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  106 QEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTK-----ELDLSDANPEVTMTMLRWIYTDELEFREDDVflTEL 180
Cdd:cd18337    20 HKQLCDVVLVAGDRRIPAHRLVLSSVSDYFAAMFTNDVReakqeEIKMEGVEPNALWALVQYAYTGRLELKEDNI--ECL 97
                          90       100       110
                  ....*....|....*....|....*....|
gi 767992314  181 MKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18337    98 LSTACLLQLSQVVEACCKFLMKQLHPSNCL 127
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
812-841 2.82e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.82e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 767992314    812 DGQTPLHLAASWGLEETVQCLLEFGANVNA 841
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
769-954 2.95e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 48.22  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  769 QTLLHRAIDENNEPTACFLIRSGCDVNSPRQ-----PGANGEGeeeARDGQTPLHLAASWGLEETVQCLLEFGA-NVNAQ 842
Cdd:cd22194   142 QTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnPKYKHEG---FYFGETPLALAACTNQPEIVQLLMEKEStDITSQ 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  843 DAEGRTPIHVAIS------SQHGVIIQL----LVSHPDIHLN-VRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVd 911
Cdd:cd22194   219 DSRGNTVLHALVTvaedskTQNDFVKRMydmiLLKSENKNLEtIRNNEGLTPLQLAAKMGKAEILKYILSREIKEKPNR- 297
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767992314  912 NKGRNFLHVA-------------VQNSDIESVLFLISVHANVNSRvQDASKLTPLH 954
Cdd:cd22194   298 SLSRKFTDWAygpvssslydltnVDTTTDNSVLEIIVYNTNIDNR-HEMLTLEPLH 352
BTB_POZ_TDPOZ cd18344
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
100-208 3.01e-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: 3.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  100 VADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIYTDELEFREDD 174
Cdd:cd18344    14 LGELWENSLFTDCCLLVAGHEFRAHKAILAARSPVFRAMFEHEMEErlknpIEIHDLDPQVFKEMMGFIYTGKAPHLHSH 93
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767992314  175 VFLTELMKLANRFQLQLLRERCEKGVMSLVNVRN 208
Cdd:cd18344    94 SMACDVLAAADKYGLEGLKVLCEDALCRNLSVEN 127
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
769-969 3.56e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 48.22  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  769 QTLLHRA---IDENNEPTACFLIrSGCDVNSPRQPGANGEGEEEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQdae 845
Cdd:cd22194    95 KTCLMKAllnINENTKEIVRILL-AFAEENGILDRFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAH--- 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  846 grtpihvaissQHGVIIQLLVSHPDIHLnvrdrqGLTPFACAMTFKNNKSAEAILKRESGAAEQVDNKGRNFLHVAVQNS 925
Cdd:cd22194   171 -----------AKGVFFNPKYKHEGFYF------GETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVTVA 233
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767992314  926 D---------IESVLFLISVHANVN-SRVQDASKLTPLHLAVQAGSEIIVRNLL 969
Cdd:cd22194   234 EdsktqndfvKRMYDMILLKSENKNlETIRNNEGLTPLQLAAKMGKAEILKYIL 287
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
914-1099 4.27e-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: 47.70  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  914 GRNFLHVAVQNSDIESVLFLI-SVHANVNSRVqdASKL----TPLHLAVQAGSEIIVRNLLLAGAKVNeltKHRQTA--- 985
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMeAAPELVNEPM--TSDLyqgeTALHIAVVNQNLNLVRELIARGADVV---SPRATGtff 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  986 --------------LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMhgrlnnirvlltectvdaeafnlrgqs 1051
Cdd:cd22192   126 rpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL--------------------------- 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767992314 1052 plhilgQYGKENAAAIFDLFLECMPG---YPLDK-PDADGSTVLLLAYMKGN 1099
Cdd:cd22192   179 ------QPNKTFACQMYDLILSYDKEddlQPLDLvPNNQGLTPFKLAAKEGN 224
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
871-1024 4.51e-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: 4.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   871 IHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQvdnkGRNFLHVAVQNsdIESVLFLISVHANVNSRVQDASKL 950
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLE--YVDAVEAILLHLLAAFRKSGPLEL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   951 -------------TPLHLAVQAGSEIIVRNLLLAGAKV------NELTK--------HRQTALHLAAQQDLPTICSVLLE 1003
Cdd:TIGR00870  117 andqytseftpgiTALHLAAHRQNYEIVKLLLERGASVparacgDFFVKsqgvdsfyHGESPLNAAACLGSPSIVALLSE 196
                          170       180
                   ....*....|....*....|.
gi 767992314  1004 NGVDFAAVDENGNNALHLAVM 1024
Cdd:TIGR00870  197 DPADILTADSLGNTLLHLLVM 217
PHA02878 PHA02878
ankyrin repeat protein; Provisional
296-451 6.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  296 HNGDLALDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLIKNGAFVNAATLGAQeTPLHlVALY 375
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN-TPLH-ISVG 243
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314  376 SSKKHSadvmsemaqIAEALLQAGANPNMQDS-KGRTPLHVSIMagNEYVFSQLLQCKQlDLELKDHEGSTALWLAV 451
Cdd:PHA02878  244 YCKDYD---------ILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGA-DINSLNSYKLTPLSSAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
592-840 6.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  592 AIAYNHPDVVSVILeqkanalhatnNLQIIPDFSLKDSRDQTVLGLALwtgMHTIAAQLLGSGAAINDTMSDG-QTLLHM 670
Cdd:PHA02875    9 AILFGELDIARRLL-----------DIGINPNFEIYDGISPIKLAMKF---RDSEAIKLLMKHGAIPDVKYPDiESELHD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  671 AIQRQDSKSALFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTL 750
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  751 VRHgcdatcwgpgpggclqtllhraidennepTACFLIRSGCdvnsprqpgangegeeeardGQTPLHLAASWGLEETVQ 830
Cdd:PHA02875  155 IDH-----------------------------KACLDIEDCC--------------------GCTPLIIAMAKGDIAICK 185
                         250
                  ....*....|
gi 767992314  831 CLLEFGANVN 840
Cdd:PHA02875  186 MLLDSGANID 195
BTB_POZ_BTBD6 cd18349
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
103-196 7.39e-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: 7.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  103 LYEQEQYSDLKIKVG----DRHISAHKFVLAARSDSWS---LANLSSTK-ELDLSDANPEVTMTMLRWIYTDELEFREDD 174
Cdd:cd18349     2 MFNNELMADVHFIVGppgaSQRVPAHKYVLAVGSSVFYamfYGDLAEVKsEIHIPDVEPAAFLILLKYMYSDEIDLEADT 81
                          90       100
                  ....*....|....*....|..
gi 767992314  175 VFLTelMKLANRFQLQLLRERC 196
Cdd:cd18349    82 VLAT--LYAAKKYIVPALAKAC 101
BTB_POZ_ZBTB44 cd18228
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
94-176 7.72e-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: 43.70  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   94 SRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDsWSLANL---SSTKELDLSDANP------EVTMT----ML 160
Cdd:cd18228     4 QELLGKLNSLRNEGHFCDVTIRVQDKIFRAHKVVLAACSD-FFRSKLvgqASPRLVLVSPAGKcvldlhHVTVTgfapLL 82
                          90
                  ....*....|....*.
gi 767992314  161 RWIYTDELEFREDDVF 176
Cdd:cd18228    83 EYAYTSTLSINTENII 98
FYVE_CARP cd15750
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...
1153-1202 1.04e-04

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: 40.81  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767992314 1153 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEipiikfdlNKPVRVCNIC 1202
Cdd:cd15750     3 CESCGAKFSVFKRKRTCADCKRYFCSNCLSKE--------ERGRRRCRRC 44
Ank_5 pfam13857
Ankyrin repeats (many copies);
975-1022 1.21e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.21e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767992314   975 VNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLA 1022
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 ...
96-209 1.61e-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: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   96 LLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLA---NLSSTKEL--DLSDANPEVTMTMLRWIYTDELEF 170
Cdd:cd18253     5 ILQVFNEFRDSRLFTDVIICVEGREFPCHRAILSACSSYFRAMfcnDHRESREMlvEINGILAEAMDCFLQYVYTGKVKI 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767992314  171 REDDVflTELMKLANRFQLQLLRERCEKGVMSLVNVRNC 209
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 ...
82-196 1.89e-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: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   82 QANKESSSESFisrllaivADLYEQEQYSDLKIKVGD----RHISAHKFVLAARS---DSWSLANLSSTK-ELDLSDANP 153
Cdd:cd18347     3 QATKPTVQERF--------AFLFNNEVLSDVHFLVGKglgsQRIPAHRFVLAVGSavfDAMFNGGMATTStEIELPDVEP 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767992314  154 EVTMTMLRWIYTDELEFREDDVFLTelMKLANRFQLQLLRERC 196
Cdd:cd18347    75 AAFLALLKFLYSDEVQIGPETVMTT--LYTAKKYAVPALEAHC 115
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
812-841 2.20e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 2.20e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 767992314   812 DGQTPLHLAASWGLEETVQCLLEFGANVNA 841
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
911-1036 2.26e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  911 DNKGRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKhrQTALHLAA 990
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVH--IRDANGNTALWNAISAKHHKIFRILYHFASISDPHAA--GDLLCTAA 630
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767992314  991 QQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLT 1036
Cdd:PLN03192  631 KRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
BACK smart00875
BTB And C-terminal Kelch; The BACK domain is found juxtaposed to the BTB domain; they are ...
209-277 2.33e-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: 41.56  E-value: 2.33e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314    209 CIRFYQTAEELNASTLMNYCAEIIASHWDDLRK-EDFSSMSAQLLYKMIKSKTeyplhkaIKVEREDVVF 277
Cdd:smart00875    1 CLGIRRFADAHGLEELAEKALRFILQNFSEVSSsEEFLELPLEQLLELLSSDD-------LNVSSEEEVF 63
BTB_POZ_BAB-like cd18315
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
109-188 2.71e-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: 41.00  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  109 YSDLKIKVGDRHISAHKFVLAARSDSWS--LANLSSTKELDLS--DANPEVTMTMLRWIYTDELEFREDDvfLTELMKLA 184
Cdd:cd18315     1 LVDVTLACEGGSLKAHKLVLAAASPYFAalLKETPPDEHPVIIlpDVPYSELKALLDFIYTGEVNVSQEQ--LESLLKLA 78

                  ....
gi 767992314  185 NRFQ 188
Cdd:cd18315    79 ELLQ 82
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
667-903 2.88e-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: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   667 LLHMAIQRQDSKSALFLLEHQADINVsrtqdGETALqLAIRNQLPLVVDAIctrgADMSVPDEKGNPPLWLALAnnledi 746
Cdd:TIGR00870   56 LFVAAIENENLELTELLLNLSCRGAV-----GDTLL-HAISLEYVDAVEAI----LLHLLAAFRKSGPLELAND------ 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   747 astlvRHGCDATcwgpgPGgclQTLLHRAIDENNEPTACFLIRSGCDVN----------SPRQPGAngegeeeaRDGQTP 816
Cdd:TIGR00870  120 -----QYTSEFT-----PG---ITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSF--------YHGESP 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   817 LHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHV--------------AISSQHGVIIQLLVSHPDIHLN-VRDRQGL 881
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLlvmenefkaeyeelSCQMYNFALSLLDKLRDSKELEvILNHQGL 258
                          250       260
                   ....*....|....*....|..
gi 767992314   882 TPFACAMTFKNNKSAEAILKRE 903
Cdd:TIGR00870  259 TPLKLAAKEGRIVLFRLKLAIK 280
BTB_POZ_KLHL12_C3IP1_DKIR cd18242
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
89-209 3.06e-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: 3.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   89 SESFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSD------SWSLANlSSTKELDLSDANPEVTMTMLRW 162
Cdd:cd18242     1 TNSHAKSILNTMNSLRKSNTLCDVTLRVEGKEFPAHRIVLAACSDyfcamfTSEMSE-KGKSEVELQGLTASTMEILLDF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767992314  163 IYTDELEFREDDVflTELMKLANRFQLQLLRERCEKGVMSLVNVRNC 209
Cdd:cd18242    80 VYTETVHVTVENV--QELLPAACLLQLKGVKQACCEFLESQLDPSNC 124
BTB_POZ_KLHL2-like cd18235
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
94-196 3.70e-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: 41.64  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   94 SRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW-----SLANLSSTKELDLSDANPEVTMTMLRWIYTDEL 168
Cdd:cd18235     6 QKAFDVMNELRKQNLLCDVILVADGVEIPAHRVVLASCSPYFhamftGDLSESRANRVTLQDVDGKALLLLIDYVYTAEI 85
                          90       100
                  ....*....|....*....|....*...
gi 767992314  169 EFREDDVflTELMKLANRFQLQLLRERC 196
Cdd:cd18235    86 QVTEENV--QVLLPAANLLQLTDVRDAC 111
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
392-452 3.75e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 3.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992314  392 AEALLQAGANPNMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQlDLELKDHEGSTALWLAVQ 452
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLELAEE 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
811-853 4.42e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.42e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 767992314   811 RDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVA 853
Cdd:pfam13857   14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
261-403 4.51e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  261 EYPLHKAikVEREDVVFLYLIEMDSQLPGKLNEADHNGDLALdLALSRRLEsIATTLVSHKADVDMVDKSGWSLLHKGIQ 340
Cdd:PHA02875   69 ESELHDA--VEEGDVKAVEELLDLGKFADDVFYKDGMTPLHL-ATILKKLD-IMKLLIARGADPDIPNTDKFSPLHLAVM 144
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767992314  341 RGDLFAATFLIKNGAFVNAATlGAQETPLhLVALysSKKHSAdvmsemaqIAEALLQAGANPN 403
Cdd:PHA02875  145 MGDIKGIELLIDHKACLDIED-CCGCTPL-IIAM--AKGDIA--------ICKMLLDSGANID 195
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
769-903 4.75e-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: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  769 QTLLHRAIDENNEPTACFLIRSGCDVNSprqpGANGEGEEEARD------GQTPLHLAASWGLEETVQCLLE---FGANV 839
Cdd:cd22196    95 QTALHIAIERRNMHLVELLVQNGADVHA----RASGEFFKKKKGgpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADI 170
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767992314  840 NAQDAEGRTPIH--VAISSQ------------HGVIIQLLVSHPDIHL-NVRDRQGLTPFACAMTFKNNKSAEAILKRE 903
Cdd:cd22196   171 SARDSMGNTVLHalVEVADNtpentkfvtkmyNEILILGAKIRPLLKLeEITNKKGLTPLKLAAKTGKIGIFAYILGRE 249
PHA02736 PHA02736
Viral ankyrin protein; Provisional
811-887 5.04e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.79  E-value: 5.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  811 RDGQTPLHLAASWGL---EETVQCLLEFGANVNAQDA-EGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFAC 886
Cdd:PHA02736   53 RHGKQCVHIVSNPDKadpQEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYV 132

                  .
gi 767992314  887 A 887
Cdd:PHA02736  133 A 133
BTB_POZ_calicin cd18307
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
109-196 6.45e-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: 40.17  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  109 YSDLKIKVGDRHISAHKFVLAARS----DSWSLANLSSTKEL----DLSDANPEVTMTMLRWIYTDELEFREDDVflTEL 180
Cdd:cd18307     1 FCDVVISVDNHSFAAHRNVLAAVSpfvkSLISSNDMKATDELsitiDCDYLSPETVEQLLDYFYTGKIVISEKNV--EDL 78
                          90
                  ....*....|....*.
gi 767992314  181 MKLANRFQLQLLRERC 196
Cdd:cd18307    79 LKGAKYFNIPRLKDHC 94
Ank_5 pfam13857
Ankyrin repeats (many copies);
832-884 6.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 6.96e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767992314   832 LLEFG-ANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPdIHLNVRDRQGLTPF 884
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTAL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
518-726 7.07e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  518 FLATNGAHVNHRNKWGETPLHTACRHGLANLTAELLQQGanpnlqteealplpkeaasltSLADSVHLQ---TPLHMAIA 594
Cdd:PHA02875   53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG---------------------KFADDVFYKdgmTPLHLATI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  595 YNHPDVVSVILEQKANalhatnnlqiiPDFSLKDSrdQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQR 674
Cdd:PHA02875  112 LKKLDIMKLLIARGAD-----------PDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767992314  675 QDSKSALFLLEHQADIN-VSRTQDgETALQLAIRNQLPLVVDAICTRGADMSV 726
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 ...
103-197 8.07e-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: 40.54  E-value: 8.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  103 LYEQEQY------SDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKELDLSDAN-P----EVTMTMLRWIYTDELEFR 171
Cdd:cd18352     1 VYLGEQYvnnatlSDVTFLVEGRRFYAHRIALLASSDAFRAMFDGGYREKEARDIEiPnirwEVFELMMRFIYTGSVDIT 80
                          90       100
                  ....*....|....*....|....*.
gi 767992314  172 EDDVFltELMKLANRFQLQLLRERCE 197
Cdd:cd18352    81 NDIAK--DLLRAADQYLLEGLKRLCE 104
PHA02875 PHA02875
ankyrin repeat protein; Provisional
547-757 8.47e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 8.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  547 NLTAELLQQGANPNLQTEEALPLPKEAASLTslaDSVHLQTPL-HMAIA-YNHPDVVS----VILEQKANALHATNNL-Q 619
Cdd:PHA02875   16 DIARRLLDIGINPNFEIYDGISPIKLAMKFR---DSEAIKLLMkHGAIPdVKYPDIESelhdAVEEGDVKAVEELLDLgK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  620 IIPDFSLKDSrdQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsrtQD-- 697
Cdd:PHA02875   93 FADDVFYKDG--MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI---EDcc 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767992314  698 GETALQLAIRNQLPLVVDAICTRGADmsvPDEKGNPP----LWLALANNLEDIASTLVRHGCDA 757
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGADC 228
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
818-887 8.50e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 8.50e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767992314  818 HLAASwGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQH-GVIIQLLVSHPDIHLnvRDRQGLTPFACA 887
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHvQVVRVLLEFGADPTL--LDKDGKTPLELA 155
BTB_POZ_KLHL3 cd18339
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
91-196 9.93e-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: 9.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   91 SFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSL-----ANLSSTKELDLSDANPEVTMTMLRWIYT 165
Cdd:cd18339     3 AHMKKAFKVMNELRSKQLLCDVTIVAEDVEIEAHRVVLAACSPYFCAmftgdMSESKAKKIEIKDVDGQTLSKLIDYIYT 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 767992314  166 DELEFREDDVFLteLMKLANRFQLQLLRERC 196
Cdd:cd18339    83 AEIEVTEENVQV--LLPAASLLQLMDVRQNC 111
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
331-450 1.18e-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: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  331 GWSLLHKGIQRGDLFAATFLIKNGAFVNAATLGA------------QETPLHLVALYSSKkhsadvmsemaQIAEALLQA 398
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgnlfyfGELPLSLAACTNQE-----------EIVRLLLEN 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  399 GANP---NMQDSKGRTPLHVSIMAGNEYVFSQLLQCKQLDL---------------ELKDHEGSTALWLA 450
Cdd:cd21882   142 GAQPaalEAQDSLGNTVLHALVLQADNTPENSAFVCQMYNLllsygahldptqqleEIPNHQGLTPLKLA 211
PHA02798 PHA02798
ankyrin-like protein; Provisional
745-1007 1.19e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  745 DIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNE-PTACFLIRSGCDVNsprqpgangegeEEARDGQTPLHLAASW 823
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDYKHMlDIVKILIENGADIN------------KKNSDGETPLYCLLSN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  824 GL---EETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV---IIQLLV-SHPDIHLnVRDRQGLTPFACAMTFKNNKSA 896
Cdd:PHA02798  120 GYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLeKGVDINT-HNNKEKYDTLHCYFKYNIDRID 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  897 EAILKR--ESGAAEQVDNKG--RNFLHVAVQ----NSDIES-VLFLISVHANVNSRvqDASKLTPLHLAVQAGSEIIVRN 967
Cdd:PHA02798  199 ADILKLfvDNGFIINKENKShkKKFMEYLNSllydNKRFKKnILDFIFSYIDINQV--DELGFNPLYYSVSHNNRKIFEY 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767992314  968 LLLAGAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVD 1007
Cdd:PHA02798  277 LLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
BTB_POZ_KLHL21 cd18250
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
96-209 1.20e-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: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   96 LLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLA-----NLSSTKELDLSDANPEVTMTMLRWIYTDELEF 170
Cdd:cd18250     8 LLRGLSELRAERKFFDVTLCAGGREFPCHRTVLAAASSYFRAMfagelRESRADRVVLHGVSAEILGLLLDFSYTGRVTV 87
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767992314  171 REDDVFLteLMKLANRFQLQLLRERCEKGVMSLVNVRNC 209
Cdd:cd18250    88 TQDNVEA--LLRAADLFQFPSVKEACCAYLQQRLDVSNC 124
Ank_5 pfam13857
Ankyrin repeats (many copies);
526-567 1.22e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 767992314   526 VNHRNKWGETPLHTACRHGLANLTAELLQQGANPNLQTEEAL 567
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGL 50
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
293-452 1.64e-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: 42.82  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  293 EADHNGDLALDLALSRRLESIATTLVSHKADVDMVDKsgwsllhkgiqrGDLFAATFliKNGAFVNAatlgaqETPLHLV 372
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAK------------GVFFNPKY--KHEGFYFG------ETPLALA 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  373 ALysskkhsadvmSEMAQIAEALLQAGANP-NMQDSKGRTPLHVSIMAG------NEYVFSQ----LLQCKQLDLE-LKD 440
Cdd:cd22194   196 AC-----------TNQPEIVQLLMEKESTDiTSQDSRGNTVLHALVTVAedsktqNDFVKRMydmiLLKSENKNLEtIRN 264
                         170
                  ....*....|..
gi 767992314  441 HEGSTALWLAVQ 452
Cdd:cd22194   265 NEGLTPLQLAAK 276
BTB_POZ cd01165
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
113-187 1.84e-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: 38.42  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  113 KIKVGDRHISAHKFVLAARS-----DSWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVFltELMKLANRF 187
Cdd:cd01165     2 VLVVEGEKFHVNKELLAQSSeyfraLFRGGFRESGQAEINLRDISPEDFRALLEFLYGGKRDLDASNLL--ELLEAANFL 79
PHA02884 PHA02884
ankyrin repeat protein; Provisional
745-853 1.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.89  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  745 DIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegEEEARdgQTPLHLAASWG 824
Cdd:PHA02884   47 DIIDAILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRY---------AEEAK--ITPLYISVLHG 115
                          90       100
                  ....*....|....*....|....*....
gi 767992314  825 LEETVQCLLEFGANVNAQDAEGRTPIHVA 853
Cdd:PHA02884  116 CLKCLEILLSYGADINIQTNDMVTPIELA 144
Ank_5 pfam13857
Ankyrin repeats (many copies);
655-705 1.99e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.99e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767992314   655 AAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLA 705
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
349-415 2.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 2.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767992314  349 FLIKNGAFVNAATLGAQETPLHLVALYSSkkhsaDVMSEMAQIaeaLLQAGANPNMQDSKGRTPLHV 415
Cdd:PHA02859   71 FLIENGADVNFKTRDNNLSALHHYLSFNK-----NVEPEILKI---LIDSGSSITEEDEDGKNLLHM 129
Ank_5 pfam13857
Ankyrin repeats (many copies);
937-989 2.27e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767992314   937 HANVNSRVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLA 989
Cdd:pfam13857    4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
BTB_POZ_NPR_plant cd18310
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
106-192 2.28e-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: 39.60  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  106 QEQYSDLKIKVGD-RHISAHKFVLAARSDS-----WSLANLSSTK--ELDLSDANP------EVTMTMLRWIYTDELEFR 171
Cdd:cd18310    15 DLFYSDAEIIVEGgRPVPVHRCILAARSPFfrdifASAKAEGANTkpKLELRELIPggivgyDAFMLVLSYLYSGRLRLV 94
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767992314  172 EDDV------------------FLTELMKLANRFQLQLL 192
Cdd:cd18310    95 PKEGsacvdsdcwhvacrpavdFALEVLYAASVFQIPEL 133
BTB_POZ_ZBTB40 cd18225
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
91-189 2.41e-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: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   91 SFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSW-SLANLSSTKELDLSDANPEVTMTMLRWIYTDELE 169
Cdd:cd18225     5 NYSRQLLQQLHTLRKEQQFCDCTIFIGTFHFRAHKLVLAASSLLFkSLLDSTDTISIDASVVSPEEFALLLEMVYTGKLP 84
                          90       100
                  ....*....|....*....|
gi 767992314  170 FREDDvfLTELMKLANRFQL 189
Cdd:cd18225    85 PGKHN--FTKIISVADSLQM 102
BTB2_POZ_IBtk cd18302
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
110-208 2.67e-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: 38.88  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  110 SDLKIKVGD-RHISAHKFVLAARSD------SWSLANLSSTKELDLsDANPEVTMTMLRWIYTDE---LEFREDDVFLTE 179
Cdd:cd18302     6 YDVTIVSEDgKEFPCHKCVLVARLEyfhsmlSSSWIEASSCSALTM-PIPSDILEIILDYLYTDEasaVKESQNVEFLCN 84
                          90       100
                  ....*....|....*....|....*....
gi 767992314  180 LMKLANRFQLQLLRERCEKGVMSLVNVRN 208
Cdd:cd18302    85 VLVIADQLLITRLKEICEVALVELLSLKN 113
BTB_POZ_KLHL38 cd18268
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
90-210 3.00e-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: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   90 ESFISRLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWSLANLSSTKE-----LDLSDANPEVTMTMLRWIY 164
Cdd:cd18268     4 QDLSSELLRQLNSLRQERILTDVILCTGDKEIPCHRNVLASSSPYFRAMFCNNFREssqakVDLKGIDSDVLDQIVDYVY 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767992314  165 TDELEFREDDVFltELMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18268    84 TGEILITRDNVL--PLMEAASMLQYPKLFEACSLYLQDQLTPENCL 127
Ank_4 pfam13637
Ankyrin repeats (many copies);
301-351 3.07e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 3.07e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767992314   301 ALDLALSRRLESIATTLVSHKADVDMVDKSGWSLLHKGIQRGDLFAATFLI 351
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
BTB_POZ_ABTB2_BPOZ2 cd18350
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
110-210 3.84e-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: 39.06  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  110 SDLKIKVGDRHISAHKFVLAARSDSWS--LANLS-----STKELDLSDANPEVTMTMLRWIY---TDELEFREDDVFltE 179
Cdd:cd18350    25 SDVTFLVEGKLFYAHKVLLVTASNRFKslLTNKSeqesqGSKTIEISDIKYHIFQMLMQYLYyggTESMEIPIADVL--E 102
                          90       100       110
                  ....*....|....*....|....*....|.
gi 767992314  180 LMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18350   103 LLSAASLFQLDALQRHCEILCSQTINLENAV 133
BTB_POZ_BTBD12_SLX4 cd18288
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
93-197 4.02e-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: 38.60  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   93 ISRLLAIVADLYEQEQYSDLKIKV-GDRHISAHKFVLAAR---------SDSWSLAN--LSSTKELDLSDANPEVTMTML 160
Cdd:cd18288     2 LGKLAADFSAMVNNPHLSDVQFQTdSGEVLYAHSFVLYARcplliqmvhSEGFSVEEegGVTTRRVLLGDVSGEAARCFL 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767992314  161 RWIYTDELEFREDdvFLTELMKLANRFQLQLLRERCE 197
Cdd:cd18288    82 QYLYTADTGLPPG--LSPHVSELADRFGVSELVHLCE 116
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
951-1073 4.26e-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: 41.28  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  951 TPLHLAVQAGSEIIVRNLLLAGAKVNELTKHR--------------QTALHLAAQQDLPTICSVLLENG-VDFAAVDENG 1015
Cdd:cd22194   143 TALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKEsTDITSQDSRG 222
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767992314 1016 NNALHLAVM-----HGRLNNIRVLLTECTVDAEAFNL------RGQSPLHILGQYGKenaAAIFDLFLE 1073
Cdd:cd22194   223 NTVLHALVTvaedsKTQNDFVKRMYDMILLKSENKNLetirnnEGLTPLQLAAKMGK---AEILKYILS 288
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
533-561 4.62e-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: 4.62e-03
                            10        20
                    ....*....|....*....|....*....
gi 767992314    533 GETPLHTACRHGLANLTAELLQQGANPNL 561
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
263-438 4.65e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  263 PLHKAIKVEREDVVFL-YLIEMDSqlpgKLNEADHNGDLALD-LALSRRL-ESIATTLVSHKADVDMVDKSGWSLLHK-- 337
Cdd:PHA03095  155 PLAVLLKSRNANVELLrLLIDAGA----DVYAVDDRFRSLLHhHLQSFKPrARIVRELIRAGCDPAATDMLGNTPLHSma 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  338 ---GIQRGDLFaatFLIKNGAFVNAATLGAQeTPLHLVALYSSKkhsadvmseMAqiAEALLQAGANPNMQDSKGRTPLH 414
Cdd:PHA03095  231 tgsSCKRSLVL---PLLIAGISINARNRYGQ-TPLHYAAVFNNP---------RA--CRRLIALGADINAVSSDGNTPLS 295
                         170       180
                  ....*....|....*....|....
gi 767992314  415 VSIMAGNEYVFSQLLQcKQLDLEL 438
Cdd:PHA03095  296 LMVRNNNGRAVRAALA-KNPSAET 318
PHA02874 PHA02874
ankyrin repeat protein; Provisional
918-1128 5.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  918 LHVAVQNSDIESVLFLISVHAN-VNSRVQDASklTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPT 996
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETT--TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  997 ICSVLLENGVDFA------------------AVDENGNNA-----LHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPL 1053
Cdd:PHA02874   83 IIKLLIDNGVDTSilpipciekdmiktildcGIDVNIKDAelktfLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPI 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767992314 1054 HILGqygKENAAAIFDLFLEcmpgypldkpdadgstvlllaymkgnanlcraivrSGARLGVNNNQGVNIFNYQV 1128
Cdd:PHA02874  162 HIAI---KHNFFDIIKLLLE-----------------------------------KGAYANVKDNNGESPLHNAA 198
BTB1_POZ_BTBD8 cd18285
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
103-165 5.51e-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: 37.71  E-value: 5.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767992314  103 LYEQEQYSDLKIKVGDRHISAHKFVLAARSD---SWSLANLSSTKELDLSD-ANPEVT--MTMLRWIYT 165
Cdd:cd18285     9 LLREELHTDVTFYVGSTLFKAHKAILLARVPeffSHIIGKLSSLEDQEPINiENLEASefKTFLRQVYT 77
BTB2_POZ_ABTB1_BPOZ1 cd18296
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
109-198 6.09e-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: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  109 YSDLKIKVGDRHISAHKFVLAARSD----------SWSLANLSSTKELDLSDANPEVTMTMLRWIYTDELEFREDDVFlt 178
Cdd:cd18296    17 FPDVCFQVEGHRFPCHKAFFCGRSDyfkallrdhfAESEENNGSIPVVTLHDVSPEVFAIVLYYIYTDDTDLPPENAY-- 94
                          90       100
                  ....*....|....*....|
gi 767992314  179 ELMKLANRFQLQLLRERCEK 198
Cdd:cd18296    95 DVLYVADMYLLPGLKRLCGT 114
PHA02946 PHA02946
ankyin-like protein; Provisional
649-856 6.47e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 6.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  649 QLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRTQDGETALQLA-IRNQLPLVVDAICTRGADMSVP 727
Cdd:PHA02946   57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSgTDDEVIERINLLVQYGAKINNS 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  728 -DEKGNPPLwLALANNLEDIASTLVRHGCDATC---WGpgpggclQTLLHRAIDENN--EPTACFLIRSGCdvnSPRQPG 801
Cdd:PHA02946  137 vDEEGCGPL-LACTDPSERVFKKIMSIGFEARIvdkFG-------KNHIHRHLMSDNpkASTISWMMKLGI---SPSKPD 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767992314  802 angegeeeaRDGQTPLHLAASWGLEET-VQCLLEFGANVNAQDAEGRTPIHVAISS 856
Cdd:PHA02946  206 ---------HDGNTPLHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT 252
Ank_4 pfam13637
Ankyrin repeats (many copies);
914-969 6.70e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 6.70e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767992314   914 GRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLL 969
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADIN--AVDGNGETALHFAASNGNVEVLKLLL 54
BTB_POZ_KBTBD11 cd18275
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
111-209 6.77e-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: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  111 DLKIKVGDRHISAHKFVLAARSDSWSlANLSStKELDLSDANPEVTMTMLRWIYTDELEFREDDVflTELMKLANRFQLQ 190
Cdd:cd18275     6 DLVIEVSGQRIRAHKSVLAAKSDYFR-ARLSR-DILKVKGLSYATLRLLVDYVYSGRMAVSKDNV--VEVVAGARFLQMP 81
                          90
                  ....*....|....*....
gi 767992314  191 LLRERCEKGVMSLVNVRNC 209
Cdd:cd18275    82 CAAQCAVDAVRAQLCLGNC 100
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
951-1061 7.21e-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: 40.55  E-value: 7.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  951 TPLHLAVQAGSEIIVRNLLLAGAKVNELTKHR--------------QTALHLAAQQDLPTICSVLLENG---VDFAAVDE 1013
Cdd:cd22193    78 TALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENEhqpADIEAQDS 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767992314 1014 NGNNALHLAVM---HGRLNNIRV------LLTEC-----TVDAEA-FNLRGQSPLHILGQYGK 1061
Cdd:cd22193   158 RGNTVLHALVTvadNTKENTKFVtrmydmILIRGaklcpTVELEEiRNNDGLTPLQLAAKMGK 220
Ank_4 pfam13637
Ankyrin repeats (many copies);
770-833 9.09e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 9.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767992314   770 TLLHRAIDENNEPTACFLIRSGCDVNspRQPGangegeeearDGQTPLHLAASWGLEETVQCLL 833
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADIN--AVDG----------NGETALHFAASNGNVEVLKLLL 54
BTB_POZ_KLHL31_KBTBD1 cd18260
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
95-210 9.66e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 31 (KLHL31); KLHL31 is also called BTB and kelch domain-containing protein 6 (BKLHD6), Kelch repeat and BTB domain-containing protein 1 (KBTBD1), or Kelch-like protein KLHL. It is a transcriptional repressor in the MAPK/JNK signaling pathway to regulate cellular functions. Overexpression inhibits the transcriptional activities of both the TPA-response element (TRE) and serum response element (SRE). It is also a novel modulator of canonical Wnt signaling, which is important for vertebrate myogenesis. It 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: 349569 [Multi-domain]  Cd Length: 120  Bit Score: 37.49  E-value: 9.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314   95 RLLAIVADLYEQEQYSDLKIKVGDRHISAHKFVLAARSDSWS--LANLSSTKELDLSDANPEVTMTMLRWIYTDELEFRE 172
Cdd:cd18260     4 NLLEGLNRMRQERFLCDLTIATKTKSFDVHKVVMASCSEYFRniLKKDPSLQRVELNDISPLGLATVITYAYTGKLTLSL 83
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767992314  173 DDVFLTelMKLANRFQLQLLRERCEKGVMSLVNVRNCI 210
Cdd:cd18260    84 YTIGST--ISAASYLQIHALVKMCCDFLMQEMNVENCM 119
PHA02989 PHA02989
ankyrin repeat protein; Provisional
786-1126 9.92e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.11  E-value: 9.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  786 FLIRSGCDVNsprqpgangegeeEARDGQTPL--HLAASWGLEETVQCLLEFGANVNAQdAEGRTPIHVAI------SSQ 857
Cdd:PHA02989   21 FLLRTGFDVN-------------EEYRGNSILllYLKRKDVKIKIVKLLIDNGADVNYK-GYIETPLCAVLrnreitSNK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  858 HGVIIQLLVSHpDIHLNVRDRQGLTPFACAMTFKNnksaeailkresgaaeqvdnkgrnflhvaVQNSDIesVLFLISVH 937
Cdd:PHA02989   87 IKKIVKLLLKF-GADINLKTFNGVSPIVCFIYNSN-----------------------------INNCDM--LRFLLSKG 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314  938 ANVNSrVQDASKLTPLHLAVQAGS--EIIVRNLLLAGAKVNELTK-HRQTALHLAAQQDLPTI----CSVLLENGVDFaa 1010
Cdd:PHA02989  135 INVND-VKNSRGYNLLHMYLESFSvkKDVIKILLSFGVNLFEKTSlYGLTPMNIYLRNDIDVIsikvIKYLIKKGVNI-- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767992314 1011 vdeNGNNALHLAVMHGRLNNIRVLLTECT---------VDAEAFNLRGQSPLHILGQYGKENAaaiFDLFLecMPGYPLD 1081
Cdd:PHA02989  212 ---ETNNNGSESVLESFLDNNKILSKKEFkvlnfilkyIKINKKDKKGFNPLLISAKVDNYEA---FNYLL--KLGDDIY 283
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 767992314 1082 KPDADGSTVLLLAYMKGNANLCRAIVrsgaRLGVNNNQGVNIFNY 1126
Cdd:PHA02989  284 NVSKDGDTVLTYAIKHGNIDMLNRIL----QLKPGKYLIKKTFEY 324
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH