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Conserved domains on  [gi|1063720694|ref|NP_001329387|]
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Beige/BEACH and WD40 domain-containing protein [Arabidopsis thaliana]

Protein Classification

PH and BEACH domain-containing protein( domain architecture ID 13153032)

PH (Pleckstrin Homology) and Beige and Chediak Higashi (BEACH) domain-containing protein with WD40 repeats, such as Arabidopsis thaliana protein SPIRRIG which is involved in cell morphogenesis; has an N-terminal region with partial similarity to a LamG domain; may be involved in protein binding and in facilitating membrane-dependent cellular processes

Gene Ontology:  GO:0005515
PubMed:  23521701|10322433

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 2957-3237 7.29e-179

Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the highly homologous CHS protein. The BEACH domain is usually followed by a series of WD repeats. The function of the BEACH domain is unknown.


:

Pssm-ID: 214982  Cd Length: 280  Bit Score: 549.90  E-value: 7.29e-179
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694  2957 TKRWQNGEISNFQYLMHLNTLAGRGYSDLTQYPVFPWILADYDGESLDLSDPNNFRKLDKPMGCQTPEGEEEFRKRYESW 3036
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694  3037 DDPEVPQFHYGSHYSSAGIVLFYLIRLPPFSAENQKLQGGQFDHADRLFNSIRETWLSAAgKGNTSDVKELIPEFFYMPE 3116
Cdd:smart01026   81 EDPDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSAS-LESMTDVKELIPEFFYLPE 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694  3117 FLENRFNLDLGEKQSGDKVGDVILPPWARGSVREFIRKHREALESDYVSENLHHWIDLIFGHKQRGKAAENAVNVFYHYT 3196
Cdd:smart01026  160 FLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFHPLT 239

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 1063720694  3197 YEGNVDVDAVTDPAMKASILAQINHFGQTPKQLFQKPHVKR 3237
Cdd:smart01026  240 YEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2756-2922 1.63e-26

Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in several eukaroyotic proteins CHS, neurobeachin (Nbea), LRBA (also called BGL, beige-like, or CDC4L), FAN, KIAA1607, and LvsA-LvsF. CHS is a rare, autosomal recessive disorder that can cause severe immunodeficiency and albinism in mammals and beige is the name for the CHS disease in mice. The CHS disease is associated with the presence of giant, perinuclear vesicles (lysosomes, melanosomes, and others) and CHS protein is thought to play an important role in the fusion, fission, or trafficking of these vesicles. All BEACH proteins contain the following domains: PH, BEACH, and WD40. The WD40 domain is involved in mediating protein-protein interactions involved in targeting proteins to subcellular compartments. The combined PH-BEACH motifs may present a single continuous structural unit involved in protein binding. Some members have an additional N-terminal Laminin G-like (LamG) domains Ca++ mediated receptors or an additional C-terminal FYVE zinc-binding domain which targets proteins to membrane lipids via interaction with phosphatidylinositol-3-phosphate, PI3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 275391  Cd Length: 112  Bit Score: 106.55  E-value: 1.63e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 2756 EKIRFRYNCERVVGLDKHDGIFLIGELCLYVIENFYIDDHGCICEKECEDELSIIDqaqglkkqfhgslesksksstlws 2835
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVVINSQKVLSYKE------------------------ 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 2836 ttikigavggrawaygggawgkekvrvtgnlpHPWHMWKLDSVHEILKRDYELRRVAVEIFSMDGCNDLLVFHKKEREEV 2915
Cdd:cd01201     57 --------------------------------HLVFKWSLSDIREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDV 104


                   ....*..
gi 1063720694 2916 FRNLLAM 2922
Cdd:cd01201    105 YKKLLSL 111
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3297-3552 1.86e-18

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 88.93  E-value: 1.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3297 GFPDRTLRFMSYDQDKLLSTHENlHEGNqIQCAGVSHDGRIVVTGAEDGLVSVWRVSKDgprgsrrlRLEKSLCAHTAKV 3376
Cdd:cd00200     69 GSSDKTIRLWDLETGECVRTLTG-HTSY-VSSVAFSPDGRILSSSSRDKTIKVWDVETG--------KCLTTLRGHTDWV 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3377 ICLRVSQPYMMIASSSDDCTVIIWDLSSLSFVRQLPNFSVPVTVVYINDLTGEIVTAAG-SVLAVWSINGDCLSVVNTSQ 3455
Cdd:cd00200    139 NSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGH 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3456 lpTDLIVSVAGSTFSDWLettwyVTGHQSGALKVWRMVHCTdpvsvpsktpsnrtgglnlgnqkpeykllLHKELKFHKQ 3535
Cdd:cd00200    219 --ENGVNSVAFSPDGYLL-----ASGSEDGTIRVWDLRTGE-----------------------------CVQTLSGHTN 262

                          250
                   ....*....|....*..
gi 1063720694 3536 PVTSLHLTTDLKQLLSG 3552
Cdd:cd00200    263 SVTSLAWSPDGKRLASG 279
Laminin_G_3 super family cl48183
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 1145-1239 5.19e-04

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


The actual alignment was detected with superfamily member pfam13385:

Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 43.14  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 1145 SNGSPSYaELYFQEDGILTLATSNSNSLSF---SGLETEEGKWHHLAVVhskpnalaglFQASVAYVYIDGKLRHMGKLG 1221
Cdd:pfam13385   40 SSGGGGY-SLGLDGDGRLRFAVNGGNGGWDtvtSGASVPLGQWTHVAVT----------YDGGTLRLYVNGVLVGSSTLT 108

                           90
                   ....*....|....*...
gi 1063720694 1222 YSPSPVGKSLqVIIGTSA 1239
Cdd:pfam13385  109 GGPPPGTGGP-LYIGRSP 125
 
Name Accession Description Interval E-value
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 2957-3237 7.29e-179

Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the highly homologous CHS protein. The BEACH domain is usually followed by a series of WD repeats. The function of the BEACH domain is unknown.


Pssm-ID: 214982  Cd Length: 280  Bit Score: 549.90  E-value: 7.29e-179
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694  2957 TKRWQNGEISNFQYLMHLNTLAGRGYSDLTQYPVFPWILADYDGESLDLSDPNNFRKLDKPMGCQTPEGEEEFRKRYESW 3036
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694  3037 DDPEVPQFHYGSHYSSAGIVLFYLIRLPPFSAENQKLQGGQFDHADRLFNSIRETWLSAAgKGNTSDVKELIPEFFYMPE 3116
Cdd:smart01026   81 EDPDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSAS-LESMTDVKELIPEFFYLPE 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694  3117 FLENRFNLDLGEKQSGDKVGDVILPPWARGSVREFIRKHREALESDYVSENLHHWIDLIFGHKQRGKAAENAVNVFYHYT 3196
Cdd:smart01026  160 FLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFHPLT 239

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 1063720694  3197 YEGNVDVDAVTDPAMKASILAQINHFGQTPKQLFQKPHVKR 3237
Cdd:smart01026  240 YEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach pfam02138
Beige/BEACH domain;
2958-3237 9.55e-177

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 543.61  E-value: 9.55e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 2958 KRWQNGEISNFQYLMHLNTLAGRGYSDLTQYPVFPWILADYDGESLDLSDPNNFRKLDKPMGCQTPEGEEEFRKRYESWD 3037
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3038 DPEvPQFHYGSHYSSAGIVLFYLIRLPPFSAENQKLQGGQFDHADRLFNSIRETWLSAAGkgNTSDVKELIPEFFYMPEF 3117
Cdd:pfam02138   81 DDD-PPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSASN--STSDVKELIPEFFYLPEF 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3118 LENRFNLDLGEKQSGDKVGDVILPPWARGSVREFIRKHREALESDYVSENLHHWIDLIFGHKQRGKAAENAVNVFYHYTY 3197
Cdd:pfam02138  158 LLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPLTY 237

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1063720694 3198 EGNVDVDAVTDPAMKASILAQINHFGQTPKQLFQKPHVKR 3237
Cdd:pfam02138  238 EGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 2957-3237 6.00e-152

BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in a family of proteins conserved throughout eukaryotes. This group contains human lysosomal trafficking regulator (LYST), LPS-responsive and beige-like anchor (LRBA) and neurobeachin. Disruption of LYST leads to Chediak-Higashi syndrome, characterized by severe immunodeficiency, albinism, poor blood coagulation and neurologic problems. Neurobeachin is a candidate gene linked to autism. LBRA seems to be upregulated in several cancer types. It has been shown that the BEACH domain itself is important for the function of these proteins.


Pssm-ID: 100117 [Multi-domain]  Cd Length: 275  Bit Score: 472.50  E-value: 6.00e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 2957 TKRWQNGEISNFQYLMHLNTLAGRGYSDLTQYPVFPWILADYDGESLDLSDPNNFRKLDKPMGCQTPEGEEEFRKRYESW 3036
Cdd:cd06071      1 TKKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERYESD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3037 DDPEVPQFHYGSHYSSAGIVLFYLIRLPPFSAENQKLQGGQFDHADRLFNSIRETWLSAAgkGNTSDVKELIPEFFYMPE 3116
Cdd:cd06071     81 SDDSDPPFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSAS--ENPSDVKELIPEFYYLPE 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3117 FLENRFNLDLGeKQSGDKVGDVILPPWARGSvREFIRKHREALESDYVSENLHHWIDLIFGHKQRGKAAENAVNVFYHYT 3196
Cdd:cd06071    159 FFLNINKFDFG-KQDGEKVNDVELPPWAKSP-EEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFHPLT 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1063720694 3197 YEGNVDVDAVTdpAMKASILAQINHFGQTPKQLFQKPHVKR 3237
Cdd:cd06071    237 YEGSVDLDSID--VEREAIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2756-2922 1.63e-26

Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in several eukaroyotic proteins CHS, neurobeachin (Nbea), LRBA (also called BGL, beige-like, or CDC4L), FAN, KIAA1607, and LvsA-LvsF. CHS is a rare, autosomal recessive disorder that can cause severe immunodeficiency and albinism in mammals and beige is the name for the CHS disease in mice. The CHS disease is associated with the presence of giant, perinuclear vesicles (lysosomes, melanosomes, and others) and CHS protein is thought to play an important role in the fusion, fission, or trafficking of these vesicles. All BEACH proteins contain the following domains: PH, BEACH, and WD40. The WD40 domain is involved in mediating protein-protein interactions involved in targeting proteins to subcellular compartments. The combined PH-BEACH motifs may present a single continuous structural unit involved in protein binding. Some members have an additional N-terminal Laminin G-like (LamG) domains Ca++ mediated receptors or an additional C-terminal FYVE zinc-binding domain which targets proteins to membrane lipids via interaction with phosphatidylinositol-3-phosphate, PI3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275391  Cd Length: 112  Bit Score: 106.55  E-value: 1.63e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 2756 EKIRFRYNCERVVGLDKHDGIFLIGELCLYVIENFYIDDHGCICEKECEDELSIIDqaqglkkqfhgslesksksstlws 2835
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVVINSQKVLSYKE------------------------ 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 2836 ttikigavggrawaygggawgkekvrvtgnlpHPWHMWKLDSVHEILKRDYELRRVAVEIFSMDGCNDLLVFHKKEREEV 2915
Cdd:cd01201     57 --------------------------------HLVFKWSLSDIREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDV 104


                   ....*..
gi 1063720694 2916 FRNLLAM 2922
Cdd:cd01201    105 YKKLLSL 111
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3297-3552 1.86e-18

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 88.93  E-value: 1.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3297 GFPDRTLRFMSYDQDKLLSTHENlHEGNqIQCAGVSHDGRIVVTGAEDGLVSVWRVSKDgprgsrrlRLEKSLCAHTAKV 3376
Cdd:cd00200     69 GSSDKTIRLWDLETGECVRTLTG-HTSY-VSSVAFSPDGRILSSSSRDKTIKVWDVETG--------KCLTTLRGHTDWV 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3377 ICLRVSQPYMMIASSSDDCTVIIWDLSSLSFVRQLPNFSVPVTVVYINDLTGEIVTAAG-SVLAVWSINGDCLSVVNTSQ 3455
Cdd:cd00200    139 NSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGH 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3456 lpTDLIVSVAGSTFSDWLettwyVTGHQSGALKVWRMVHCTdpvsvpsktpsnrtgglnlgnqkpeykllLHKELKFHKQ 3535
Cdd:cd00200    219 --ENGVNSVAFSPDGYLL-----ASGSEDGTIRVWDLRTGE-----------------------------CVQTLSGHTN 262

                          250
                   ....*....|....*..
gi 1063720694 3536 PVTSLHLTTDLKQLLSG 3552
Cdd:cd00200    263 SVTSLAWSPDGKRLASG 279
WD40 COG2319
WD40 repeat [General function prediction only];
3300-3573 2.76e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.11  E-value: 2.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3300 DRTLRFMSYDQDKLLSTHENlHEGnQIQCAGVSHDGRIVVTGAEDGLVSVWRVSKDgprgsrrlRLEKSLCAHTAKVICL 3379
Cdd:COG2319    141 DGTVRLWDLATGKLLRTLTG-HSG-AVTSVAFSPDGKLLASGSDDGTVRLWDLATG--------KLLRTLTGHTGAVRSV 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3380 RVS---QpymMIASSSDDCTVIIWDLSSLSFVRQLPNFSVPVT-VVYINDltGEIVTAAGS--VLAVWSINGDclSVVNT 3453
Cdd:COG2319    211 AFSpdgK---LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRsVAFSPD--GRLLASGSAdgTVRLWDLATG--ELLRT 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3454 SQLPTDLIVSVAgstFS---DWLettwyVTGHQSGALKVWRMvhctdpvsvpsktpsnRTGglnlgnqkpeyKLLlhKEL 3530
Cdd:COG2319    284 LTGHSGGVNSVA---FSpdgKLL-----ASGSDDGTVRLWDL----------------ATG-----------KLL--RTL 326

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1063720694 3531 KFHKQPVTSLHLTTDLKQLLSGDSAGHLLSWTVPDEILKASLK 3573
Cdd:COG2319    327 TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLT 369
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 2867-2920 1.26e-06

PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the Beige/BEACH domain (pfam02138), it immediately precedes the Beige/BEACH domain.


Pssm-ID: 434260  Cd Length: 99  Bit Score: 49.18  E-value: 1.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1063720694 2867 PHPWHmWKLDSVHEILKRDYELRRVAVEIFSMDGCNDLLVF-HKKEREEVFRNLL 2920
Cdd:pfam14844   46 PKHKR-WPISDIKEVHLRRYLLRDTALEIFLIDRTSLFFNFpDTGTRRKVYRKLV 99
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 3326-3445 3.07e-05

Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.


Pssm-ID: 466575 [Multi-domain]  Cd Length: 350  Bit Score: 49.30  E-value: 3.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3326 IQCAGVSHDGRIVVTGAEDGLVSVWRVSKDGP--RGSRRLRLEKS-------------LCAHTAKVICLRVSQPYMMIAS 3390
Cdd:pfam20426  127 VSCVAVTSDGSILATGSYDTTVMVWEVLRGRSseKRSRNTQTEFPrkdhviaetpfhiLCGHDDIITCLYVSVELDIVIS 206

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063720694 3391 SSDDCTVIIWDLSSLSFVRQL--PNFSvPVTVVYINDlTGEIVTAAGSVLA--VWSING 3445
Cdd:pfam20426  207 GSKDGTCIFHTLREGRYVRSIrhPSGC-PLSKLVASR-HGRIVLYADDDLSlhLYSING 263
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3364-3401 1.11e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.91  E-value: 1.11e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1063720694  3364 RLEKSLCAHTAKVICLRVSQPYMMIASSSDDCTVIIWD 3401
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 1145-1239 5.19e-04

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 43.14  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 1145 SNGSPSYaELYFQEDGILTLATSNSNSLSF---SGLETEEGKWHHLAVVhskpnalaglFQASVAYVYIDGKLRHMGKLG 1221
Cdd:pfam13385   40 SSGGGGY-SLGLDGDGRLRFAVNGGNGGWDtvtSGASVPLGQWTHVAVT----------YDGGTLRLYVNGVLVGSSTLT 108

                           90
                   ....*....|....*...
gi 1063720694 1222 YSPSPVGKSLqVIIGTSA 1239
Cdd:pfam13385  109 GGPPPGTGGP-LYIGRSP 125
 
Name Accession Description Interval E-value
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 2957-3237 7.29e-179

Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the highly homologous CHS protein. The BEACH domain is usually followed by a series of WD repeats. The function of the BEACH domain is unknown.


Pssm-ID: 214982  Cd Length: 280  Bit Score: 549.90  E-value: 7.29e-179
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694  2957 TKRWQNGEISNFQYLMHLNTLAGRGYSDLTQYPVFPWILADYDGESLDLSDPNNFRKLDKPMGCQTPEGEEEFRKRYESW 3036
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694  3037 DDPEVPQFHYGSHYSSAGIVLFYLIRLPPFSAENQKLQGGQFDHADRLFNSIRETWLSAAgKGNTSDVKELIPEFFYMPE 3116
Cdd:smart01026   81 EDPDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSAS-LESMTDVKELIPEFFYLPE 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694  3117 FLENRFNLDLGEKQSGDKVGDVILPPWARGSVREFIRKHREALESDYVSENLHHWIDLIFGHKQRGKAAENAVNVFYHYT 3196
Cdd:smart01026  160 FLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFHPLT 239

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|.
gi 1063720694  3197 YEGNVDVDAVTDPAMKASILAQINHFGQTPKQLFQKPHVKR 3237
Cdd:smart01026  240 YEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach pfam02138
Beige/BEACH domain;
2958-3237 9.55e-177

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 543.61  E-value: 9.55e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 2958 KRWQNGEISNFQYLMHLNTLAGRGYSDLTQYPVFPWILADYDGESLDLSDPNNFRKLDKPMGCQTPEGEEEFRKRYESWD 3037
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3038 DPEvPQFHYGSHYSSAGIVLFYLIRLPPFSAENQKLQGGQFDHADRLFNSIRETWLSAAGkgNTSDVKELIPEFFYMPEF 3117
Cdd:pfam02138   81 DDD-PPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSASN--STSDVKELIPEFFYLPEF 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3118 LENRFNLDLGEKQSGDKVGDVILPPWARGSVREFIRKHREALESDYVSENLHHWIDLIFGHKQRGKAAENAVNVFYHYTY 3197
Cdd:pfam02138  158 LLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPLTY 237

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1063720694 3198 EGNVDVDAVTDPAMKASILAQINHFGQTPKQLFQKPHVKR 3237
Cdd:pfam02138  238 EGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 2957-3237 6.00e-152

BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in a family of proteins conserved throughout eukaryotes. This group contains human lysosomal trafficking regulator (LYST), LPS-responsive and beige-like anchor (LRBA) and neurobeachin. Disruption of LYST leads to Chediak-Higashi syndrome, characterized by severe immunodeficiency, albinism, poor blood coagulation and neurologic problems. Neurobeachin is a candidate gene linked to autism. LBRA seems to be upregulated in several cancer types. It has been shown that the BEACH domain itself is important for the function of these proteins.


Pssm-ID: 100117 [Multi-domain]  Cd Length: 275  Bit Score: 472.50  E-value: 6.00e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 2957 TKRWQNGEISNFQYLMHLNTLAGRGYSDLTQYPVFPWILADYDGESLDLSDPNNFRKLDKPMGCQTPEGEEEFRKRYESW 3036
Cdd:cd06071      1 TKKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERYESD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3037 DDPEVPQFHYGSHYSSAGIVLFYLIRLPPFSAENQKLQGGQFDHADRLFNSIRETWLSAAgkGNTSDVKELIPEFFYMPE 3116
Cdd:cd06071     81 SDDSDPPFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSAS--ENPSDVKELIPEFYYLPE 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3117 FLENRFNLDLGeKQSGDKVGDVILPPWARGSvREFIRKHREALESDYVSENLHHWIDLIFGHKQRGKAAENAVNVFYHYT 3196
Cdd:cd06071    159 FFLNINKFDFG-KQDGEKVNDVELPPWAKSP-EEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFHPLT 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1063720694 3197 YEGNVDVDAVTdpAMKASILAQINHFGQTPKQLFQKPHVKR 3237
Cdd:cd06071    237 YEGSVDLDSID--VEREAIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2756-2922 1.63e-26

Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in several eukaroyotic proteins CHS, neurobeachin (Nbea), LRBA (also called BGL, beige-like, or CDC4L), FAN, KIAA1607, and LvsA-LvsF. CHS is a rare, autosomal recessive disorder that can cause severe immunodeficiency and albinism in mammals and beige is the name for the CHS disease in mice. The CHS disease is associated with the presence of giant, perinuclear vesicles (lysosomes, melanosomes, and others) and CHS protein is thought to play an important role in the fusion, fission, or trafficking of these vesicles. All BEACH proteins contain the following domains: PH, BEACH, and WD40. The WD40 domain is involved in mediating protein-protein interactions involved in targeting proteins to subcellular compartments. The combined PH-BEACH motifs may present a single continuous structural unit involved in protein binding. Some members have an additional N-terminal Laminin G-like (LamG) domains Ca++ mediated receptors or an additional C-terminal FYVE zinc-binding domain which targets proteins to membrane lipids via interaction with phosphatidylinositol-3-phosphate, PI3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275391  Cd Length: 112  Bit Score: 106.55  E-value: 1.63e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 2756 EKIRFRYNCERVVGLDKHDGIFLIGELCLYVIENFYIDDHGCICEKECEDELSIIDqaqglkkqfhgslesksksstlws 2835
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVVINSQKVLSYKE------------------------ 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 2836 ttikigavggrawaygggawgkekvrvtgnlpHPWHMWKLDSVHEILKRDYELRRVAVEIFSMDGCNDLLVFHKKEREEV 2915
Cdd:cd01201     57 --------------------------------HLVFKWSLSDIREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDV 104


                   ....*..
gi 1063720694 2916 FRNLLAM 2922
Cdd:cd01201    105 YKKLLSL 111
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3297-3552 1.86e-18

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 88.93  E-value: 1.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3297 GFPDRTLRFMSYDQDKLLSTHENlHEGNqIQCAGVSHDGRIVVTGAEDGLVSVWRVSKDgprgsrrlRLEKSLCAHTAKV 3376
Cdd:cd00200     69 GSSDKTIRLWDLETGECVRTLTG-HTSY-VSSVAFSPDGRILSSSSRDKTIKVWDVETG--------KCLTTLRGHTDWV 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3377 ICLRVSQPYMMIASSSDDCTVIIWDLSSLSFVRQLPNFSVPVTVVYINDLTGEIVTAAG-SVLAVWSINGDCLSVVNTSQ 3455
Cdd:cd00200    139 NSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTGKCLGTLRGH 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3456 lpTDLIVSVAGSTFSDWLettwyVTGHQSGALKVWRMVHCTdpvsvpsktpsnrtgglnlgnqkpeykllLHKELKFHKQ 3535
Cdd:cd00200    219 --ENGVNSVAFSPDGYLL-----ASGSEDGTIRVWDLRTGE-----------------------------CVQTLSGHTN 262

                          250
                   ....*....|....*..
gi 1063720694 3536 PVTSLHLTTDLKQLLSG 3552
Cdd:cd00200    263 SVTSLAWSPDGKRLASG 279
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3321-3572 1.57e-15

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 80.07  E-value: 1.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3321 HEGnQIQCAGVSHDGRIVVTGAEDGLVSVWRVSKDgprgsrrlRLEKSLCAHTAKVICLRVSQPYMMIASSSDDCTVIIW 3400
Cdd:cd00200      8 HTG-GVTCVAFSPDGKLLATGSGDGTIKVWDLETG--------ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLW 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3401 DLSSLSFVRQLPNFSVPVT-VVYINDltGEIVTAAGS--VLAVWSI-NGDCLSVVNTsqlPTDLIVSVAGSTFSDWLett 3476
Cdd:cd00200     79 DLETGECVRTLTGHTSYVSsVAFSPD--GRILSSSSRdkTIKVWDVeTGKCLTTLRG---HTDWVNSVAFSPDGTFV--- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3477 wyVTGHQSGALKVWRMvhctdpvsvpsktpsnRTGGLNlgnqkpeyklllhKELKFHKQPVTSLHLTTDLKQLLSGDSAG 3556
Cdd:cd00200    151 --ASSSQDGTIKLWDL----------------RTGKCV-------------ATLTGHTGEVNSVAFSPDGEKLLSSSSDG 199

                          250
                   ....*....|....*.
gi 1063720694 3557 HLLSWTVPDEILKASL 3572
Cdd:cd00200    200 TIKLWDLSTGKCLGTL 215
WD40 COG2319
WD40 repeat [General function prediction only];
3300-3573 2.76e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.11  E-value: 2.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3300 DRTLRFMSYDQDKLLSTHENlHEGnQIQCAGVSHDGRIVVTGAEDGLVSVWRVSKDgprgsrrlRLEKSLCAHTAKVICL 3379
Cdd:COG2319    141 DGTVRLWDLATGKLLRTLTG-HSG-AVTSVAFSPDGKLLASGSDDGTVRLWDLATG--------KLLRTLTGHTGAVRSV 210

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3380 RVS---QpymMIASSSDDCTVIIWDLSSLSFVRQLPNFSVPVT-VVYINDltGEIVTAAGS--VLAVWSINGDclSVVNT 3453
Cdd:COG2319    211 AFSpdgK---LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRsVAFSPD--GRLLASGSAdgTVRLWDLATG--ELLRT 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3454 SQLPTDLIVSVAgstFS---DWLettwyVTGHQSGALKVWRMvhctdpvsvpsktpsnRTGglnlgnqkpeyKLLlhKEL 3530
Cdd:COG2319    284 LTGHSGGVNSVA---FSpdgKLL-----ASGSDDGTVRLWDL----------------ATG-----------KLL--RTL 326

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1063720694 3531 KFHKQPVTSLHLTTDLKQLLSGDSAGHLLSWTVPDEILKASLK 3573
Cdd:COG2319    327 TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLT 369
WD40 COG2319
WD40 repeat [General function prediction only];
3300-3492 1.58e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 75.72  E-value: 1.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3300 DRTLRFMSYDQDKLLSTHEnlHEGNQIQCAGVSHDGRIVVTGAEDGLVSVWRVSkdgprGSRRLRLeksLCAHTAKVICL 3379
Cdd:COG2319    225 DGTVRLWDLATGKLLRTLT--GHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-----TGELLRT---LTGHSGGVNSV 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3380 RVSQPYMMIASSSDDCTVIIWDLSSLSFVRQLPNFSVPVT-VVYINDltGEIVtAAGS---VLAVWSINGdcLSVVNTSQ 3455
Cdd:COG2319    295 AFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRsVAFSPD--GKTL-ASGSddgTVRLWDLAT--GELLRTLT 369

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1063720694 3456 LPTDLIVSVAGSTFSDWLettwyVTGHQSGALKVWRM 3492
Cdd:COG2319    370 GHTGAVTSVAFSPDGRTL-----ASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3300-3442 1.24e-12

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 71.60  E-value: 1.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3300 DRTLRFMSYDQDKLLSTHENlHEGNqIQCAGVSHDGRIVVTGAEDGLVSVWRVSKDgprgsrrlRLEKSLCAHTAKVICL 3379
Cdd:cd00200    156 DGTIKLWDLRTGKCVATLTG-HTGE-VNSVAFSPDGEKLLSSSSDGTIKLWDLSTG--------KCLGTLRGHENGVNSV 225

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063720694 3380 RVSQPYMMIASSSDDCTVIIWDLSSLSFVRQLPNFSVPVTVVYINDLTGEIVTAA--GSVLaVWS 3442
Cdd:cd00200    226 AFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSadGTIR-IWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
3300-3404 3.55e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 65.32  E-value: 3.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3300 DRTLRFMSYDQDKLLSTHENlhEGNQIQCAGVSHDGRIVVTGAEDGLVSVWRVskDGPRGSRRLRlekslcAHTAKVICL 3379
Cdd:COG2319    309 DGTVRLWDLATGKLLRTLTG--HTGAVRSVAFSPDGKTLASGSDDGTVRLWDL--ATGELLRTLT------GHTGAVTSV 378

                           90       100
                   ....*....|....*....|....*
gi 1063720694 3380 RVSQPYMMIASSSDDCTVIIWDLSS 3404
Cdd:COG2319    379 AFSPDGRTLASGSADGTVRLWDLAT 403
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 2867-2920 1.26e-06

PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the Beige/BEACH domain (pfam02138), it immediately precedes the Beige/BEACH domain.


Pssm-ID: 434260  Cd Length: 99  Bit Score: 49.18  E-value: 1.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1063720694 2867 PHPWHmWKLDSVHEILKRDYELRRVAVEIFSMDGCNDLLVF-HKKEREEVFRNLL 2920
Cdd:pfam14844   46 PKHKR-WPISDIKEVHLRRYLLRDTALEIFLIDRTSLFFNFpDTGTRRKVYRKLV 99
WD40 COG2319
WD40 repeat [General function prediction only];
3329-3573 6.69e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.45  E-value: 6.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3329 AGVSHDGRIVVTGAEDGLVSVWRVskdgprgsRRLRLEKSLCAHTAKVICLRVSQPYMMIASSSDDCTVIIWDLSSLSFV 3408
Cdd:COG2319     42 LAASPDGARLAAGAGDLTLLLLDA--------AAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLL 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3409 RQLPNFSVPVTVVYINDLTGEIVTA-AGSVLAVWSI-NGDCLSVVNTsqlPTDLIVSVAgstFS---DWLettwyVTGHQ 3483
Cdd:COG2319    114 RTLTGHTGAVRSVAFSPDGKTLASGsADGTVRLWDLaTGKLLRTLTG---HSGAVTSVA---FSpdgKLL-----ASGSD 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3484 SGALKVWRMvhctdpvsvpsktpsnRTGglnlgnqkpeyKLLlhKELKFHKQPVTSLHLTTDLKQLLSGDSAGHLLSWTV 3563
Cdd:COG2319    183 DGTVRLWDL----------------ATG-----------KLL--RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233

                          250
                   ....*....|
gi 1063720694 3564 PDEILKASLK 3573
Cdd:COG2319    234 ATGKLLRTLT 243
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 3326-3445 3.07e-05

Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.


Pssm-ID: 466575 [Multi-domain]  Cd Length: 350  Bit Score: 49.30  E-value: 3.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 3326 IQCAGVSHDGRIVVTGAEDGLVSVWRVSKDGP--RGSRRLRLEKS-------------LCAHTAKVICLRVSQPYMMIAS 3390
Cdd:pfam20426  127 VSCVAVTSDGSILATGSYDTTVMVWEVLRGRSseKRSRNTQTEFPrkdhviaetpfhiLCGHDDIITCLYVSVELDIVIS 206

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063720694 3391 SSDDCTVIIWDLSSLSFVRQL--PNFSvPVTVVYINDlTGEIVTAAGSVLA--VWSING 3445
Cdd:pfam20426  207 GSKDGTCIFHTLREGRYVRSIrhPSGC-PLSKLVASR-HGRIVLYADDDLSlhLYSING 263
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3364-3401 1.11e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.91  E-value: 1.11e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1063720694  3364 RLEKSLCAHTAKVICLRVSQPYMMIASSSDDCTVIIWD 3401
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
3364-3401 3.77e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 3.77e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1063720694 3364 RLEKSLCAHTAKVICLRVSQPYMMIASSSDDCTVIIWD 3401
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 1145-1239 5.19e-04

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 43.14  E-value: 5.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063720694 1145 SNGSPSYaELYFQEDGILTLATSNSNSLSF---SGLETEEGKWHHLAVVhskpnalaglFQASVAYVYIDGKLRHMGKLG 1221
Cdd:pfam13385   40 SSGGGGY-SLGLDGDGRLRFAVNGGNGGWDtvtSGASVPLGQWTHVAVT----------YDGGTLRLYVNGVLVGSSTLT 108

                           90
                   ....*....|....*...
gi 1063720694 1222 YSPSPVGKSLqVIIGTSA 1239
Cdd:pfam13385  109 GGPPPGTGGP-LYIGRSP 125
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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