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Conserved domains on  [gi|54292123|ref|NP_000072|]
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lysosomal-trafficking regulator [Homo sapiens]

Protein Classification

neurobeachin family protein( domain architecture ID 12912990)

neurobeachin family protein, similar to lysosomal trafficking regulating protein CHS1 (or LYST).

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 ...
 3132-3422 3.79e-162

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: 502.14  E-value: 3.79e-162
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123    3132 TNLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYKYL 3211
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123    3212 EEeyrkgareddpmPPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRLSSFESMTDVK 3291
Cdd:smart01026   81 ED------------PDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVK 148

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123    3292 ELIPEFFYLPEFLVNREGFDFGVRQNGERVNHVNLPPWARNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKAS 3371
Cdd:smart01026  149 ELIPEFFYLPEFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEA 228

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 54292123    3372 VQAINVFHPATYFG-MDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3422
Cdd:smart01026  229 VEALNVFHPLTYEGaVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 3012-3117 6.78e-30

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: 116.18  E-value: 6.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3012 ESIRVNRRCISVAPSRETAGELLLGKCGMYFVEDN------ASDTVESSSLQGELEPASFSWTYEEIKEVHKRWWQLRDN 3085
Cdd:cd01201    1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFtisedgKIVVINSQKVLSYKEHLVFKWSLSDIREVHKRRYLLRDT 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 54292123 3086 AVEIFLTNGRTLLLAFDNtKVRDDVYHNILTN 3117
Cdd:cd01201   81 ALEIFFTDGTNYFLNFPS-KERNDVYKKLLSL 111
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3529-3778 1.17e-24

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: 107.04  E-value: 1.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3529 TDIQWSA----ILSwGYADNILRLKSKQSEPPVNFIQSSQQYqVTSCAWVPDScQLFTGS----KCGV--ITAYTNRFTs 3598
Cdd:cd00200   55 RDVAASAdgtyLAS-GSSDKTIRLWDLETGECVRTLTGHTSY-VSSVAFSPDG-RILSSSsrdkTIKVwdVETGKCLTT- 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3599 stpseiemetqihLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIATvcd 3678
Cdd:cd00200  131 -------------LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLS--- 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3679 sAGGGSDLRLWTVN-----GDLVGHvhcREIICSVAFSNQPegvsiNVIAGGLENGIVRLWSTWDLKPVReiTFPKSNKP 3753
Cdd:cd00200  195 -SSSDGTIKLWDLStgkclGTLRGH---ENGVNSVAFSPDG-----YLLASGSEDGTIRVWDLRTGECVQ--TLSGHTNS 263

                        250       260
                 ....*....|....*....|....*
gi 54292123 3754 IISLTFSCDGHHLYTANSDGTVIAW 3778
Cdd:cd00200  264 VTSLAWSPDGKRLASGSADGTIRIW 288
 
Name Accession Description Interval E-value
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 3132-3422 3.79e-162

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: 502.14  E-value: 3.79e-162
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123    3132 TNLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYKYL 3211
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123    3212 EEeyrkgareddpmPPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRLSSFESMTDVK 3291
Cdd:smart01026   81 ED------------PDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVK 148

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123    3292 ELIPEFFYLPEFLVNREGFDFGVRQNGERVNHVNLPPWARNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKAS 3371
Cdd:smart01026  149 ELIPEFFYLPEFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEA 228

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 54292123    3372 VQAINVFHPATYFG-MDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3422
Cdd:smart01026  229 VEALNVFHPLTYEGaVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach pfam02138
Beige/BEACH domain;
3133-3422 2.12e-154

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 479.66  E-value: 2.12e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3133 NLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYKYLE 3212
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3213 EeyrkgareddpmpPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRLSSfESMTDVKE 3292
Cdd:pfam02138   81 D-------------DDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKE 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3293 LIPEFFYLPEFLVNREGFDFGVRQNGERVNHVNLPPWARNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKASV 3372
Cdd:pfam02138  147 LIPEFFYLPEFLLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAV 226

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 54292123   3373 QAINVFHPATYFG-MDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3422
Cdd:pfam02138  227 EALNVFHPLTYEGsVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 3132-3422 3.88e-126

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: 398.54  E-value: 3.88e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3132 TNLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYkyl 3211
Cdd:cd06071    1 TKKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERY--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3212 eeeyrkgarEDDPMPPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRlSSFESMTDVK 3291
Cdd:cd06071   78 ---------ESDSDDSDPPFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWR-SASENPSDVK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3292 ELIPEFFYLPEFLVNREGFDFGVrQNGERVNHVNLPPWArNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKAS 3371
Cdd:cd06071  148 ELIPEFYYLPEFFLNINKFDFGK-QDGEKVNDVELPPWA-KSPEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEA 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 54292123 3372 VQAINVFHPATYFGmDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3422
Cdd:cd06071  226 VKAKNVFHPLTYEG-SVDLDSIDVEREAIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 3012-3117 6.78e-30

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: 116.18  E-value: 6.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3012 ESIRVNRRCISVAPSRETAGELLLGKCGMYFVEDN------ASDTVESSSLQGELEPASFSWTYEEIKEVHKRWWQLRDN 3085
Cdd:cd01201    1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFtisedgKIVVINSQKVLSYKEHLVFKWSLSDIREVHKRRYLLRDT 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 54292123 3086 AVEIFLTNGRTLLLAFDNtKVRDDVYHNILTN 3117
Cdd:cd01201   81 ALEIFFTDGTNYFLNFPS-KERNDVYKKLLSL 111
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 3020-3115 6.18e-29

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: 112.74  E-value: 6.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3020 CISVAPSRETAGELLLGKCGMYFVED---NASDTVESSSLQGELEPASFSWTYEEIKEVHKRWWQLRDNAVEIFLTNGRT 3096
Cdd:pfam14844    1 CELVTPMGVVRGKLSITTDHIYFTADdedEALDSVQESESLGYDKPKHKRWPISDIKEVHLRRYLLRDTALEIFLIDRTS 80

                           90
                   ....*....|....*....
gi 54292123   3097 LLLAFDNTKVRDDVYHNIL 3115
Cdd:pfam14844   81 LFFNFPDTGTRRKVYRKLV 99
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3529-3778 1.17e-24

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: 107.04  E-value: 1.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3529 TDIQWSA----ILSwGYADNILRLKSKQSEPPVNFIQSSQQYqVTSCAWVPDScQLFTGS----KCGV--ITAYTNRFTs 3598
Cdd:cd00200   55 RDVAASAdgtyLAS-GSSDKTIRLWDLETGECVRTLTGHTSY-VSSVAFSPDG-RILSSSsrdkTIKVwdVETGKCLTT- 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3599 stpseiemetqihLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIATvcd 3678
Cdd:cd00200  131 -------------LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLS--- 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3679 sAGGGSDLRLWTVN-----GDLVGHvhcREIICSVAFSNQPegvsiNVIAGGLENGIVRLWSTWDLKPVReiTFPKSNKP 3753
Cdd:cd00200  195 -SSSDGTIKLWDLStgkclGTLRGH---ENGVNSVAFSPDG-----YLLASGSEDGTIRVWDLRTGECVQ--TLSGHTNS 263

                        250       260
                 ....*....|....*....|....*
gi 54292123 3754 IISLTFSCDGHHLYTANSDGTVIAW 3778
Cdd:cd00200  264 VTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
3568-3787 1.51e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 100.37  E-value: 1.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3568 VTSCAWVPDSCQLFTGSKCGVITaytnRFTSSTPSEIEmetqiHLYGHTEEITSLfvckPYS----ILISVSRDGTCIIW 3643
Cdd:COG2319  165 VTSVAFSPDGKLLASGSDDGTVR----LWDLATGKLLR-----TLTGHTGAVRSV----AFSpdgkLLASGSADGTVRLW 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3644 DLNRLCYVQSLAGHKSPVTAVSASETSGDIAtvcdSAGGGSDLRLWTVNGDLVGHV--HCREIICSVAFSnqPEGvsiNV 3721
Cdd:COG2319  232 DLATGKLLRTLTGHSGSVRSVAFSPDGRLLA----SGSADGTVRLWDLATGELLRTltGHSGGVNSVAFS--PDG---KL 302

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54292123 3722 IAGGLENGIVRLWSTWDLKPVReiTFPKSNKPIISLTFSCDGHHLYTANSDGTVIAWCRKDQQRLK 3787
Cdd:COG2319  303 LASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLR 366
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 3560-3758 1.47e-06

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: 53.54  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3560 IQSSQQYQ-VTSCAWV-PDSCQLFTGSKCGVITAY-------------TNRFTSSTPSEIEMETQIH-LYGHTEEITSLF 3623
Cdd:pfam20426  117 VQSIRQHKdVVSCVAVtSDGSILATGSYDTTVMVWevlrgrssekrsrNTQTEFPRKDHVIAETPFHiLCGHDDIITCLY 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3624 VCKPYSILISVSRDGTCIIWDLNRLCYVQSLAgHKS--PVTAVSASEtSGDIATVCDsagGGSDLRLWTVNG------DL 3695
Cdd:pfam20426  197 VSVELDIVISGSKDGTCIFHTLREGRYVRSIR-HPSgcPLSKLVASR-HGRIVLYAD---DDLSLHLYSINGkhiassES 271

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54292123   3696 VGHVHCREIICSVAFSnqpegvsinVIAGglENGIVRLWSTWDLKPVREitFPKSNKPIISLT 3758
Cdd:pfam20426  272 NGRLNCIELSSCGEFL---------VCAG--DQGQIVVRSMNSLEVVRR--YNGIGKIITSLT 321
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3612-3644 2.03e-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: 41.14  E-value: 2.03e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 54292123    3612 LYGHTEEITSLFVCKPYSILISVSRDGTCIIWD 3644
Cdd:smart00320    8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 3132-3422 3.79e-162

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: 502.14  E-value: 3.79e-162
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123    3132 TNLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYKYL 3211
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123    3212 EEeyrkgareddpmPPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRLSSFESMTDVK 3291
Cdd:smart01026   81 ED------------PDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVK 148

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123    3292 ELIPEFFYLPEFLVNREGFDFGVRQNGERVNHVNLPPWARNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKAS 3371
Cdd:smart01026  149 ELIPEFFYLPEFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEA 228

                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 54292123    3372 VQAINVFHPATYFG-MDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3422
Cdd:smart01026  229 VEALNVFHPLTYEGaVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach pfam02138
Beige/BEACH domain;
3133-3422 2.12e-154

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 479.66  E-value: 2.12e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3133 NLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYKYLE 3212
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3213 EeyrkgareddpmpPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRLSSfESMTDVKE 3292
Cdd:pfam02138   81 D-------------DDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKE 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3293 LIPEFFYLPEFLVNREGFDFGVRQNGERVNHVNLPPWARNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKASV 3372
Cdd:pfam02138  147 LIPEFFYLPEFLLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAV 226

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 54292123   3373 QAINVFHPATYFG-MDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3422
Cdd:pfam02138  227 EALNVFHPLTYEGsVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 3132-3422 3.88e-126

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: 398.54  E-value: 3.88e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3132 TNLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYkyl 3211
Cdd:cd06071    1 TKKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERY--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3212 eeeyrkgarEDDPMPPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRlSSFESMTDVK 3291
Cdd:cd06071   78 ---------ESDSDDSDPPFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWR-SASENPSDVK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3292 ELIPEFFYLPEFLVNREGFDFGVrQNGERVNHVNLPPWArNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKAS 3371
Cdd:cd06071  148 ELIPEFYYLPEFFLNINKFDFGK-QDGEKVNDVELPPWA-KSPEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEA 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 54292123 3372 VQAINVFHPATYFGmDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3422
Cdd:cd06071  226 VKAKNVFHPLTYEG-SVDLDSIDVEREAIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 3012-3117 6.78e-30

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: 116.18  E-value: 6.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3012 ESIRVNRRCISVAPSRETAGELLLGKCGMYFVEDN------ASDTVESSSLQGELEPASFSWTYEEIKEVHKRWWQLRDN 3085
Cdd:cd01201    1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFtisedgKIVVINSQKVLSYKEHLVFKWSLSDIREVHKRRYLLRDT 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 54292123 3086 AVEIFLTNGRTLLLAFDNtKVRDDVYHNILTN 3117
Cdd:cd01201   81 ALEIFFTDGTNYFLNFPS-KERNDVYKKLLSL 111
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 3020-3115 6.18e-29

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: 112.74  E-value: 6.18e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3020 CISVAPSRETAGELLLGKCGMYFVED---NASDTVESSSLQGELEPASFSWTYEEIKEVHKRWWQLRDNAVEIFLTNGRT 3096
Cdd:pfam14844    1 CELVTPMGVVRGKLSITTDHIYFTADdedEALDSVQESESLGYDKPKHKRWPISDIKEVHLRRYLLRDTALEIFLIDRTS 80

                           90
                   ....*....|....*....
gi 54292123   3097 LLLAFDNTKVRDDVYHNIL 3115
Cdd:pfam14844   81 LFFNFPDTGTRRKVYRKLV 99
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3529-3778 1.17e-24

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: 107.04  E-value: 1.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3529 TDIQWSA----ILSwGYADNILRLKSKQSEPPVNFIQSSQQYqVTSCAWVPDScQLFTGS----KCGV--ITAYTNRFTs 3598
Cdd:cd00200   55 RDVAASAdgtyLAS-GSSDKTIRLWDLETGECVRTLTGHTSY-VSSVAFSPDG-RILSSSsrdkTIKVwdVETGKCLTT- 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3599 stpseiemetqihLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIATvcd 3678
Cdd:cd00200  131 -------------LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLS--- 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3679 sAGGGSDLRLWTVN-----GDLVGHvhcREIICSVAFSNQPegvsiNVIAGGLENGIVRLWSTWDLKPVReiTFPKSNKP 3753
Cdd:cd00200  195 -SSSDGTIKLWDLStgkclGTLRGH---ENGVNSVAFSPDG-----YLLASGSEDGTIRVWDLRTGECVQ--TLSGHTNS 263

                        250       260
                 ....*....|....*....|....*
gi 54292123 3754 IISLTFSCDGHHLYTANSDGTVIAW 3778
Cdd:cd00200  264 VTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
3568-3787 1.51e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 100.37  E-value: 1.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3568 VTSCAWVPDSCQLFTGSKCGVITaytnRFTSSTPSEIEmetqiHLYGHTEEITSLfvckPYS----ILISVSRDGTCIIW 3643
Cdd:COG2319  165 VTSVAFSPDGKLLASGSDDGTVR----LWDLATGKLLR-----TLTGHTGAVRSV----AFSpdgkLLASGSADGTVRLW 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3644 DLNRLCYVQSLAGHKSPVTAVSASETSGDIAtvcdSAGGGSDLRLWTVNGDLVGHV--HCREIICSVAFSnqPEGvsiNV 3721
Cdd:COG2319  232 DLATGKLLRTLTGHSGSVRSVAFSPDGRLLA----SGSADGTVRLWDLATGELLRTltGHSGGVNSVAFS--PDG---KL 302

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 54292123 3722 IAGGLENGIVRLWSTWDLKPVReiTFPKSNKPIISLTFSCDGHHLYTANSDGTVIAWCRKDQQRLK 3787
Cdd:COG2319  303 LASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLR 366
WD40 COG2319
WD40 repeat [General function prediction only];
3568-3778 3.74e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 99.22  E-value: 3.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3568 VTSCAWVPDSCQLFTGSKCGVITAYtnrftsSTPSEIEMETqihLYGHTEEITSLFvckpYS----ILISVSRDGTCIIW 3643
Cdd:COG2319  207 VRSVAFSPDGKLLASGSADGTVRLW------DLATGKLLRT---LTGHSGSVRSVA----FSpdgrLLASGSADGTVRLW 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3644 DLNRLCYVQSLAGHKSPVTAVSASETSGDIAtvcdSAGGGSDLRLWTVN-----GDLVGHVHcreIICSVAFSnqPEGvs 3718
Cdd:COG2319  274 DLATGELLRTLTGHSGGVNSVAFSPDGKLLA----SGSDDGTVRLWDLAtgkllRTLTGHTG---AVRSVAFS--PDG-- 342

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3719 iNVIAGGLENGIVRLWSTWDLKPVReiTFPKSNKPIISLTFSCDGHHLYTANSDGTVIAW 3778
Cdd:COG2319  343 -KTLASGSDDGTVRLWDLATGELLR--TLTGHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3568-3778 3.27e-20

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: 93.94  E-value: 3.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3568 VTSCAWVPDSCQLFTGSKCGVITAYtnrftsstpsEIEMETQIH-LYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLN 3646
Cdd:cd00200   12 VTCVAFSPDGKLLATGSGDGTIKVW----------DLETGELLRtLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3647 RLCYVQSLAGHKSPVTAVSASeTSGDIATvcdsaGGGSD--LRLWTVN-----GDLVGHvhcREIICSVAFSnqPEGvsi 3719
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFS-PDGRILS-----SSSRDktIKVWDVEtgkclTTLRGH---TDWVNSVAFS--PDG--- 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 54292123 3720 NVIAGGLENGIVRLWSTWDLKPVReiTFPKSNKPIISLTFSCDGHHLYTANSDGTVIAW 3778
Cdd:cd00200  148 TFVASSSQDGTIKLWDLRTGKCVA--TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3611-3778 6.08e-19

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: 90.47  E-value: 6.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3611 HLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIAtvcdSAGGGSDLRLWT 3690
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLA----SGSSDKTIRLWD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3691 VNGD-----LVGHvhcREIICSVAFSNqpegvSINVIAGGLENGIVRLWSTWDLKPVREITFPksNKPIISLTFSCDGHH 3765
Cdd:cd00200   80 LETGecvrtLTGH---TSYVSSVAFSP-----DGRILSSSSRDKTIKVWDVETGKCLTTLRGH--TDWVNSVAFSPDGTF 149

                        170
                 ....*....|...
gi 54292123 3766 LYTANSDGTVIAW 3778
Cdd:cd00200  150 VASSSQDGTIKLW 162
WD40 COG2319
WD40 repeat [General function prediction only];
3614-3787 7.45e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 89.20  E-value: 7.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3614 GHTEEITSLFVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIAtvcdSAGGGSDLRLWTVN- 3692
Cdd:COG2319   76 GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLA----SGSADGTVRLWDLAt 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3693 ----GDLVGHvhcREIICSVAFSnqPEGvsiNVIAGGLENGIVRLWSTWDLKPVReiTFPKSNKPIISLTFSCDGHHLYT 3768
Cdd:COG2319  152 gkllRTLTGH---SGAVTSVAFS--PDG---KLLASGSDDGTVRLWDLATGKLLR--TLTGHTGAVRSVAFSPDGKLLAS 221

                        170
                 ....*....|....*....
gi 54292123 3769 ANSDGTVIAWCRKDQQRLK 3787
Cdd:COG2319  222 GSADGTVRLWDLATGKLLR 240
WD40 COG2319
WD40 repeat [General function prediction only];
3614-3787 2.35e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.41  E-value: 2.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3614 GHTEEITSLFVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIAtvcdSAGGGSDLRLWTVNG 3693
Cdd:COG2319   34 GLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLA----SASADGTVRLWDLAT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3694 -----DLVGHvhcREIICSVAFSnqPEGvsiNVIAGGLENGIVRLWSTWDLKPVReiTFPKSNKPIISLTFSCDGHHLYT 3768
Cdd:COG2319  110 glllrTLTGH---TGAVRSVAFS--PDG---KTLASGSADGTVRLWDLATGKLLR--TLTGHSGAVTSVAFSPDGKLLAS 179

                        170
                 ....*....|....*....
gi 54292123 3769 ANSDGTVIAWCRKDQQRLK 3787
Cdd:COG2319  180 GSDDGTVRLWDLATGKLLR 198
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3568-3735 7.64e-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: 69.29  E-value: 7.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3568 VTSCAWVPDSCQLFTGSKCGVITAYtnrftsSTPSEIEMETqihLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLNR 3647
Cdd:cd00200  138 VNSVAFSPDGTFVASSSQDGTIKLW------DLRTGKCVAT---LTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3648 LCYVQSLAGHKSPVTAVSASeTSGDIATVCDsaGGGS----DLRLWTVNGDLVGHvhcREIICSVAFSNqpegvSINVIA 3723
Cdd:cd00200  209 GKCLGTLRGHENGVNSVAFS-PDGYLLASGS--EDGTirvwDLRTGECVQTLSGH---TNSVTSLAWSP-----DGKRLA 277

                        170
                 ....*....|..
gi 54292123 3724 GGLENGIVRLWS 3735
Cdd:cd00200  278 SGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
3529-3693 7.03e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 58.00  E-value: 7.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3529 TDIQWSA---ILSWGYADNILRLKSKQSEPPVNFIQSsQQYQVTSCAWVPDSCQLFTGSKCGVITAYtnrftsstpsEIE 3605
Cdd:COG2319  250 RSVAFSPdgrLLASGSADGTVRLWDLATGELLRTLTG-HSGGVNSVAFSPDGKLLASGSDDGTVRLW----------DLA 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3606 METQIH-LYGHTEEITSLfVCKPY-SILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIAtvcdSAGGG 3683
Cdd:COG2319  319 TGKLLRtLTGHTGAVRSV-AFSPDgKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLA----SGSAD 393

                        170
                 ....*....|
gi 54292123 3684 SDLRLWTVNG 3693
Cdd:COG2319  394 GTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 3651-3778 1.45e-07

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: 56.19  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123 3651 VQSLAGHKSPVTAVSASETSGDIATvcdsAGGGSDLRLWTVNGD-----LVGHVHC-REIICSvAFSNQpegvsinVIAG 3724
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLAT----GSGDGTIKVWDLETGellrtLKGHTGPvRDVAAS-ADGTY-------LASG 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 54292123 3725 GlENGIVRLWSTWDLKPVReiTFPKSNKPIISLTFSCDGHHLYTANSDGTVIAW 3778
Cdd:cd00200   70 S-SDKTIRLWDLETGECVR--TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVW 120
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 3560-3758 1.47e-06

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: 53.54  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3560 IQSSQQYQ-VTSCAWV-PDSCQLFTGSKCGVITAY-------------TNRFTSSTPSEIEMETQIH-LYGHTEEITSLF 3623
Cdd:pfam20426  117 VQSIRQHKdVVSCVAVtSDGSILATGSYDTTVMVWevlrgrssekrsrNTQTEFPRKDHVIAETPFHiLCGHDDIITCLY 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292123   3624 VCKPYSILISVSRDGTCIIWDLNRLCYVQSLAgHKS--PVTAVSASEtSGDIATVCDsagGGSDLRLWTVNG------DL 3695
Cdd:pfam20426  197 VSVELDIVISGSKDGTCIFHTLREGRYVRSIR-HPSgcPLSKLVASR-HGRIVLYAD---DDLSLHLYSINGkhiassES 271

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 54292123   3696 VGHVHCREIICSVAFSnqpegvsinVIAGglENGIVRLWSTWDLKPVREitFPKSNKPIISLT 3758
Cdd:pfam20426  272 NGRLNCIELSSCGEFL---------VCAG--DQGQIVVRSMNSLEVVRR--YNGIGKIITSLT 321
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3612-3644 2.03e-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: 41.14  E-value: 2.03e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 54292123    3612 LYGHTEEITSLFVCKPYSILISVSRDGTCIIWD 3644
Cdd:smart00320    8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
3612-3644 1.99e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 1.99e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 54292123   3612 LYGHTEEITSLFVCKPYSILISVSRDGTCIIWD 3644
Cdd:pfam00400    7 LEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
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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