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Conserved domains on  [gi|767912070|ref|XP_011542335|]
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lysosomal-trafficking regulator isoform X1 [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 ...
3186-3476 4.39e-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: 501.75  E-value: 4.39e-162
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070   3186 TNLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYKYL 3265
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070   3266 EEeyrkgareddpmPPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRLSSFESMTDVK 3345
Cdd:smart01026   81 ED------------PDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVK 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070   3346 ELIPEFFYLPEFLVNREGFDFGVRQNGERVNHVNLPPWARNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKAS 3425
Cdd:smart01026  149 ELIPEFFYLPEFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEA 228
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 767912070   3426 VQAINVFHPATYFG-MDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3476
Cdd:smart01026  229 VEALNVFHPLTYEGaVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
3066-3171 5.70e-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: 5.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3066 ESIRVNRRCISVAPSRETAGELLLGKCGMYFVEDN------ASDTVESSSLQGELEPASFSWTYEEIKEVHKRWWQLRDN 3139
Cdd:cd01201     1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFtisedgKIVVINSQKVLSYKEHLVFKWSLSDIREVHKRRYLLRDT 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767912070 3140 AVEIFLTNGRTLLLAFDNtKVRDDVYHNILTN 3171
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 ...
3583-3832 1.14e-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: 453027 [Multi-domain]  Cd Length: 289  Bit Score: 107.04  E-value: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3583 TDIQWSA----ILSwGYADNILRLKSKQSEPPVNFIQSSQQYqVTSCAWVPDScQLFTGS----KCGV--ITAYTNRFTs 3652
Cdd:cd00200    55 RDVAASAdgtyLAS-GSSDKTIRLWDLETGECVRTLTGHTSY-VSSVAFSPDG-RILSSSsrdkTIKVwdVETGKCLTT- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3653 stpseiemetqihLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIATvcd 3732
Cdd:cd00200   131 -------------LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLS--- 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3733 sAGGGSDLRLWTVN-----GDLVGHvhcREIICSVAFSNQPegvsiNVIAGGLENGIVRLWSTWDLKPVReiTFPKSNKP 3807
Cdd:cd00200   195 -SSSDGTIKLWDLStgkclGTLRGH---ENGVNSVAFSPDG-----YLLASGSEDGTIRVWDLRTGECVQ--TLSGHTNS 263
                         250       260
                  ....*....|....*....|....*
gi 767912070 3808 IISLTFSCDGHHLYTANSDGTVIAW 3832
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 ...
3186-3476 4.39e-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: 501.75  E-value: 4.39e-162
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070   3186 TNLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYKYL 3265
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070   3266 EEeyrkgareddpmPPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRLSSFESMTDVK 3345
Cdd:smart01026   81 ED------------PDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVK 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070   3346 ELIPEFFYLPEFLVNREGFDFGVRQNGERVNHVNLPPWARNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKAS 3425
Cdd:smart01026  149 ELIPEFFYLPEFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEA 228
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 767912070   3426 VQAINVFHPATYFG-MDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3476
Cdd:smart01026  229 VEALNVFHPLTYEGaVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach pfam02138
Beige/BEACH domain;
3187-3476 3.97e-152

Beige/BEACH domain;


Pssm-ID: 426617  Cd Length: 276  Bit Score: 473.10  E-value: 3.97e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070  3187 NLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYKYLE 3266
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070  3267 EeyrkgareddpmpPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRLSSfESMTDVKE 3346
Cdd:pfam02138   81 D-------------DDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHADRLFHSIAEAWKSAS-NSQSDVKE 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070  3347 LIPEFFYLPEFLVNREGFDFGVRQNGeRVNHVNLPPWARNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKASV 3426
Cdd:pfam02138  147 LIPEFFYLPEFLLNSNNFDLGGRQDG-KVDDVELPPWAKGSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAV 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767912070  3427 QAINVFHPATYFG-MDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3476
Cdd:pfam02138  226 EALNVFHPLTYEGsVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 276
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
3186-3476 3.97e-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: 3.97e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3186 TNLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYkyl 3265
Cdd:cd06071     1 TKKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERY--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3266 eeeyrkgarEDDPMPPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRlSSFESMTDVK 3345
Cdd:cd06071    78 ---------ESDSDDSDPPFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWR-SASENPSDVK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3346 ELIPEFFYLPEFLVNREGFDFGVrQNGERVNHVNLPPWArNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKAS 3425
Cdd:cd06071   148 ELIPEFYYLPEFFLNINKFDFGK-QDGEKVNDVELPPWA-KSPEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEA 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767912070 3426 VQAINVFHPATYFGmDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3476
Cdd:cd06071   226 VKAKNVFHPLTYEG-SVDLDSIDVEREAIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
3066-3171 5.70e-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: 5.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3066 ESIRVNRRCISVAPSRETAGELLLGKCGMYFVEDN------ASDTVESSSLQGELEPASFSWTYEEIKEVHKRWWQLRDN 3139
Cdd:cd01201     1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFtisedgKIVVINSQKVLSYKEHLVFKWSLSDIREVHKRRYLLRDT 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767912070 3140 AVEIFLTNGRTLLLAFDNtKVRDDVYHNILTN 3171
Cdd:cd01201    81 ALEIFFTDGTNYFLNFPS-KERNDVYKKLLSL 111
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
3074-3169 5.19e-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: 113.13  E-value: 5.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070  3074 CISVAPSRETAGELLLGKCGMYFVED---NASDTVESSSLQGELEPASFSWTYEEIKEVHKRWWQLRDNAVEIFLTNGRT 3150
Cdd:pfam14844    1 CELVTPMGVVRGKLSITTDHIYFTADdedEALDSVQESESLGYDKPKHKRWPISDIKEVHLRRYLLRDTALEIFLIDRTS 80
                           90
                   ....*....|....*....
gi 767912070  3151 LLLAFDNTKVRDDVYHNIL 3169
Cdd:pfam14844   81 LFFNFPDTGTRRKVYRKLV 99
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
3583-3832 1.14e-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: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3583 TDIQWSA----ILSwGYADNILRLKSKQSEPPVNFIQSSQQYqVTSCAWVPDScQLFTGS----KCGV--ITAYTNRFTs 3652
Cdd:cd00200    55 RDVAASAdgtyLAS-GSSDKTIRLWDLETGECVRTLTGHTSY-VSSVAFSPDG-RILSSSsrdkTIKVwdVETGKCLTT- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3653 stpseiemetqihLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIATvcd 3732
Cdd:cd00200   131 -------------LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLS--- 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3733 sAGGGSDLRLWTVN-----GDLVGHvhcREIICSVAFSNQPegvsiNVIAGGLENGIVRLWSTWDLKPVReiTFPKSNKP 3807
Cdd:cd00200   195 -SSSDGTIKLWDLStgkclGTLRGH---ENGVNSVAFSPDG-----YLLASGSEDGTIRVWDLRTGECVQ--TLSGHTNS 263
                         250       260
                  ....*....|....*....|....*
gi 767912070 3808 IISLTFSCDGHHLYTANSDGTVIAW 3832
Cdd:cd00200   264 VTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
3530-3837 1.60e-16

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 85.91  E-value: 1.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3530 PSAPVPVVCFSQPHGERFGSLQALPTRAICGLSRNFCLLMTYSKEQGVRSMNSTDIQWSAILSWGYaDNILRLKSKQSEP 3609
Cdd:COG2319   154 HSESVTSLAFSPDGKLLASGSSLDGTIKLWDLRTGKPLSTLAGHTDPVSSLAFSPDGGLLIASGSS-DGTIRLWDLSTGK 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3610 PVNFIQSSQQYQVTSCaWVPDSCQLFTGSKCGVITAYTNRFTSSTPSeiemetqiHLYGHTEEITSLFVCKPYSILISVS 3689
Cdd:COG2319   233 LLRSTLSGHSDSVVSS-FSPDGSLLASGSSDGTIRLWDLRSSSSLLR--------TLSGHSSSVLSVAFSPDGKLLASGS 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3690 RDGTCIIWDL--NRLCYVQSLAGHKSPVTAVSASETSGDIATvcdsaGGGSDLRLWTVNGDLVGHVHCREI---ICSVAF 3764
Cdd:COG2319   304 SDGTVRLWDLetGKLLSSLTLKGHEGPVSSLSFSPDGSLLVS-----GGSDDGTIRLWDLRTGKPLKTLEGhsnVLSVSF 378
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912070 3765 SNqpegvSINVIAGGLENGIVRLWSTWDLKPVREitFPKSNKPIISLTFSCDGHHLYTANSDGTVIAWCRKDQ 3837
Cdd:COG2319   379 SP-----DGRVVSSGSTDGTVRLWDLSTGSLLRN--LDGHTSRVTSLDFSPDGKSLASGSSDNTIRLWDLKTS 444
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
3666-3698 1.97e-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: 1.97e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 767912070   3666 LYGHTEEITSLFVCKPYSILISVSRDGTCIIWD 3698
Cdd:smart00320    8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
3666-3698 1.94e-03

WD domain, G-beta repeat;


Pssm-ID: 425662 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 1.94e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767912070  3666 LYGHTEEITSLFVCKPYSILISVSRDGTCIIWD 3698
Cdd:pfam00400    7 LEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
3186-3476 4.39e-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: 501.75  E-value: 4.39e-162
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070   3186 TNLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYKYL 3265
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070   3266 EEeyrkgareddpmPPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRLSSFESMTDVK 3345
Cdd:smart01026   81 ED------------PDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVK 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070   3346 ELIPEFFYLPEFLVNREGFDFGVRQNGERVNHVNLPPWARNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKAS 3425
Cdd:smart01026  149 ELIPEFFYLPEFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEA 228
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|..
gi 767912070   3426 VQAINVFHPATYFG-MDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3476
Cdd:smart01026  229 VEALNVFHPLTYEGaVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach pfam02138
Beige/BEACH domain;
3187-3476 3.97e-152

Beige/BEACH domain;


Pssm-ID: 426617  Cd Length: 276  Bit Score: 473.10  E-value: 3.97e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070  3187 NLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYKYLE 3266
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070  3267 EeyrkgareddpmpPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRLSSfESMTDVKE 3346
Cdd:pfam02138   81 D-------------DDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHADRLFHSIAEAWKSAS-NSQSDVKE 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070  3347 LIPEFFYLPEFLVNREGFDFGVRQNGeRVNHVNLPPWARNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKASV 3426
Cdd:pfam02138  147 LIPEFFYLPEFLLNSNNFDLGGRQDG-KVDDVELPPWAKGSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAV 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767912070  3427 QAINVFHPATYFG-MDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3476
Cdd:pfam02138  226 EALNVFHPLTYEGsVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 276
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
3186-3476 3.97e-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: 3.97e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3186 TNLWYTGQITNFEYLTHLNKHAGRSFNDLMQYPVFPFILADYVSETLDLNDLLIYRNLSKPIAVQYKEKEDRYVDTYkyl 3265
Cdd:cd06071     1 TKKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERY--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3266 eeeyrkgarEDDPMPPVQPYHYGSHYSNSGTVLHFLVRMPPFTKMFLAYQDQSFDIPDRTFHSTNTTWRlSSFESMTDVK 3345
Cdd:cd06071    78 ---------ESDSDDSDPPFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWR-SASENPSDVK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3346 ELIPEFFYLPEFLVNREGFDFGVrQNGERVNHVNLPPWArNDPRLFILIHRQALESDYVSQNICQWIDLVFGYKQKGKAS 3425
Cdd:cd06071   148 ELIPEFYYLPEFFLNINKFDFGK-QDGEKVNDVELPPWA-KSPEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEA 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767912070 3426 VQAINVFHPATYFGmDVSAVEDPVQRRALETMIKTYGQTPRQLFHMAHVSR 3476
Cdd:cd06071   226 VKAKNVFHPLTYEG-SVDLDSIDVEREAIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
3066-3171 5.70e-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: 5.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3066 ESIRVNRRCISVAPSRETAGELLLGKCGMYFVEDN------ASDTVESSSLQGELEPASFSWTYEEIKEVHKRWWQLRDN 3139
Cdd:cd01201     1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFtisedgKIVVINSQKVLSYKEHLVFKWSLSDIREVHKRRYLLRDT 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 767912070 3140 AVEIFLTNGRTLLLAFDNtKVRDDVYHNILTN 3171
Cdd:cd01201    81 ALEIFFTDGTNYFLNFPS-KERNDVYKKLLSL 111
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
3074-3169 5.19e-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: 113.13  E-value: 5.19e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070  3074 CISVAPSRETAGELLLGKCGMYFVED---NASDTVESSSLQGELEPASFSWTYEEIKEVHKRWWQLRDNAVEIFLTNGRT 3150
Cdd:pfam14844    1 CELVTPMGVVRGKLSITTDHIYFTADdedEALDSVQESESLGYDKPKHKRWPISDIKEVHLRRYLLRDTALEIFLIDRTS 80
                           90
                   ....*....|....*....
gi 767912070  3151 LLLAFDNTKVRDDVYHNIL 3169
Cdd:pfam14844   81 LFFNFPDTGTRRKVYRKLV 99
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
3583-3832 1.14e-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: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3583 TDIQWSA----ILSwGYADNILRLKSKQSEPPVNFIQSSQQYqVTSCAWVPDScQLFTGS----KCGV--ITAYTNRFTs 3652
Cdd:cd00200    55 RDVAASAdgtyLAS-GSSDKTIRLWDLETGECVRTLTGHTSY-VSSVAFSPDG-RILSSSsrdkTIKVwdVETGKCLTT- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3653 stpseiemetqihLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIATvcd 3732
Cdd:cd00200   131 -------------LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLS--- 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3733 sAGGGSDLRLWTVN-----GDLVGHvhcREIICSVAFSNQPegvsiNVIAGGLENGIVRLWSTWDLKPVReiTFPKSNKP 3807
Cdd:cd00200   195 -SSSDGTIKLWDLStgkclGTLRGH---ENGVNSVAFSPDG-----YLLASGSEDGTIRVWDLRTGECVQ--TLSGHTNS 263
                         250       260
                  ....*....|....*....|....*
gi 767912070 3808 IISLTFSCDGHHLYTANSDGTVIAW 3832
Cdd:cd00200   264 VTSLAWSPDGKRLASGSADGTIRIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
3622-3832 3.07e-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: 3.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3622 VTSCAWVPDSCQLFTGSKCGVITAYtnrftsstpsEIEMETQIH-LYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLN 3700
Cdd:cd00200    12 VTCVAFSPDGKLLATGSGDGTIKVW----------DLETGELLRtLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3701 RLCYVQSLAGHKSPVTAVSASeTSGDIATvcdsaGGGSD--LRLWTVN-----GDLVGHvhcREIICSVAFSnqPEGvsi 3773
Cdd:cd00200    82 TGECVRTLTGHTSYVSSVAFS-PDGRILS-----SSSRDktIKVWDVEtgkclTTLRGH---TDWVNSVAFS--PDG--- 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767912070 3774 NVIAGGLENGIVRLWSTWDLKPVReiTFPKSNKPIISLTFSCDGHHLYTANSDGTVIAW 3832
Cdd:cd00200   148 TFVASSSQDGTIKLWDLRTGKCVA--TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
3665-3832 5.81e-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: 5.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3665 HLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIAtvcdSAGGGSDLRLWT 3744
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLA----SGSSDKTIRLWD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3745 VNGD-----LVGHvhcREIICSVAFSNqpegvSINVIAGGLENGIVRLWSTWDLKPVREITFPksNKPIISLTFSCDGHH 3819
Cdd:cd00200    80 LETGecvrtLTGH---TSYVSSVAFSP-----DGRILSSSSRDKTIKVWDVETGKCLTTLRGH--TDWVNSVAFSPDGTF 149
                         170
                  ....*....|...
gi 767912070 3820 LYTANSDGTVIAW 3832
Cdd:cd00200   150 VASSSQDGTIKLW 162
WD40 COG2319
WD40 repeat [General function prediction only];
3530-3837 1.60e-16

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 85.91  E-value: 1.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3530 PSAPVPVVCFSQPHGERFGSLQALPTRAICGLSRNFCLLMTYSKEQGVRSMNSTDIQWSAILSWGYaDNILRLKSKQSEP 3609
Cdd:COG2319   154 HSESVTSLAFSPDGKLLASGSSLDGTIKLWDLRTGKPLSTLAGHTDPVSSLAFSPDGGLLIASGSS-DGTIRLWDLSTGK 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3610 PVNFIQSSQQYQVTSCaWVPDSCQLFTGSKCGVITAYTNRFTSSTPSeiemetqiHLYGHTEEITSLFVCKPYSILISVS 3689
Cdd:COG2319   233 LLRSTLSGHSDSVVSS-FSPDGSLLASGSSDGTIRLWDLRSSSSLLR--------TLSGHSSSVLSVAFSPDGKLLASGS 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3690 RDGTCIIWDL--NRLCYVQSLAGHKSPVTAVSASETSGDIATvcdsaGGGSDLRLWTVNGDLVGHVHCREI---ICSVAF 3764
Cdd:COG2319   304 SDGTVRLWDLetGKLLSSLTLKGHEGPVSSLSFSPDGSLLVS-----GGSDDGTIRLWDLRTGKPLKTLEGhsnVLSVSF 378
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912070 3765 SNqpegvSINVIAGGLENGIVRLWSTWDLKPVREitFPKSNKPIISLTFSCDGHHLYTANSDGTVIAWCRKDQ 3837
Cdd:COG2319   379 SP-----DGRVVSSGSTDGTVRLWDLSTGSLLRN--LDGHTSRVTSLDFSPDGKSLASGSSDNTIRLWDLKTS 444
WD40 COG2319
WD40 repeat [General function prediction only];
3594-3832 2.71e-14

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 78.59  E-value: 2.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3594 GYADNILRLKSKQSEPPVNFIQSSQQYQVTSCAW-VPDSCQLFTGSKCGVITAYTNRFTSSTpseiemETQIHLYGHTEE 3672
Cdd:COG2319    84 SSDGTIKLWDLDNGEKLIKSLEGLHDSSVSKLALsSPDGNSILLASSSLDGTVKLWDLSTPG------KLIRTLEGHSES 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3673 ITSL-FVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHKSPVTAVSASETSGDIATvcdSAGGGSDLRLWTVNGDLVG 3751
Cdd:COG2319   158 VTSLaFSPDGKLLASGSSLDGTIKLWDLRTGKPLSTLAGHTDPVSSLAFSPDGGLLIA---SGSSDGTIRLWDLSTGKLL 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3752 HVHCREIICSVAFSNQPEGvsiNVIAGGLENGIVRLWST-WDLKPVReiTFPKSNKPIISLTFSCDGHHLYTANSDGTVI 3830
Cdd:COG2319   235 RSTLSGHSDSVVSSFSPDG---SLLASGSSDGTIRLWDLrSSSSLLR--TLSGHSSSVLSVAFSPDGKLLASGSSDGTVR 309

                  ..
gi 767912070 3831 AW 3832
Cdd:COG2319   310 LW 311
WD40 COG2319
WD40 repeat [General function prediction only];
3590-3853 3.72e-14

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 78.21  E-value: 3.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3590 ILSWGYADNILRLKSKQSEPPVNFIQSSQQYQVTSCAWVPDSCQLFTGSKCGVITAYTNRFTSSTPSEIEmetqihlyGH 3669
Cdd:COG2319   126 LLASSSLDGTVKLWDLSTPGKLIRTLEGHSESVTSLAFSPDGKLLASGSSLDGTIKLWDLRTGKPLSTLA--------GH 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3670 TEEITSL-FVCKPYSILISVSRDGTCIIWDL-NRLCYVQSLAGHKSPVTAVSASETSGDIATVCDSAgggsdLRLWTVNG 3747
Cdd:COG2319   198 TDPVSSLaFSPDGGLLIASGSSDGTIRLWDLsTGKLLRSTLSGHSDSVVSSFSPDGSLLASGSSDGT-----IRLWDLRS 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3748 D------LVGHvhcREIICSVAFSNQPegvsiNVIAGGLENGIVRLWSTWDLKPVREITFPKSNKPIISLTFSCDGHHLY 3821
Cdd:COG2319   273 SssllrtLSGH---SSSVLSVAFSPDG-----KLLASGSSDGTVRLWDLETGKLLSSLTLKGHEGPVSSLSFSPDGSLLV 344
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767912070 3822 TANS-DGTVIAWCRKDQQRLKQPMFYSFLSSYA 3853
Cdd:COG2319   345 SGGSdDGTIRLWDLRTGKPLKTLEGHSNVLSVS 377
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
3622-3789 7.23e-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: 7.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3622 VTSCAWVPDSCQLFTGSKCGVITAYtnrftsSTPSEIEMETqihLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLNR 3701
Cdd:cd00200   138 VNSVAFSPDGTFVASSSQDGTIKLW------DLRTGKCVAT---LTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3702 LCYVQSLAGHKSPVTAVSASeTSGDIATVCDsaGGGS----DLRLWTVNGDLVGHvhcREIICSVAFSNqpegvSINVIA 3777
Cdd:cd00200   209 GKCLGTLRGHENGVNSVAFS-PDGYLLASGS--EDGTirvwDLRTGECVQTLSGH---TNSVTSLAWSP-----DGKRLA 277
                         170
                  ....*....|..
gi 767912070 3778 GGLENGIVRLWS 3789
Cdd:cd00200   278 SGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
3631-3832 2.80e-11

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 68.96  E-value: 2.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3631 SCQLFTGSKCGVITAYTNRFTSSTPSEIEMETQIHLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLN--RLCYVQSL 3708
Cdd:COG2319    26 NSLSLLSLGSSESGILLLALLSDSLVSLPDLSSLLLRGHEDSITSIAFSPDGELLLSGSSDGTIKLWDLDngEKLIKSLE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3709 AGHKSPVTAVSASETSGDIATVCDSAGGGSdLRLWTVNGD------LVGHvhcREIICSVAFSNQPEgvsiNVIAGGLEN 3782
Cdd:COG2319   106 GLHDSSVSKLALSSPDGNSILLASSSLDGT-VKLWDLSTPgklirtLEGH---SESVTSLAFSPDGK----LLASGSSLD 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767912070 3783 GIVRLWSTWDLKPVReiTFPKSNKPIISLTFSCDG-HHLYTANSDGTVIAW 3832
Cdd:COG2319   178 GTIKLWDLRTGKPLS--TLAGHTDPVSSLAFSPDGgLLIASGSSDGTIRLW 226
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
3705-3832 1.31e-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: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3705 VQSLAGHKSPVTAVSASETSGDIATvcdsAGGGSDLRLWTVNGD-----LVGHVHC-REIICSvAFSNQpegvsinVIAG 3778
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLAT----GSGDGTIKVWDLETGellrtLKGHTGPvRDVAAS-ADGTY-------LASG 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767912070 3779 GlENGIVRLWSTWDLKPVReiTFPKSNKPIISLTFSCDGHHLYTANSDGTVIAW 3832
Cdd:cd00200    70 S-SDKTIRLWDLETGECVR--TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVW 120
WD40 COG2319
WD40 repeat [General function prediction only];
3588-3749 1.19e-05

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 51.24  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3588 SAILSWGYADNILRLKSKQSEPPVNFIQSSQQYQVTSCAWVPDSCQLFTGSKCGVI----------------TAYTNRFT 3651
Cdd:COG2319   253 GSLLASGSSDGTIRLWDLRSSSSLLRTLSGHSSSVLSVAFSPDGKLLASGSSDGTVrlwdletgkllssltlKGHEGPVS 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912070 3652 SSTPSE-------------------IEMETQIHLYGHTEEITSLFVCKPYSILISVSRDGTCIIWDLNRLCYVQSLAGHK 3712
Cdd:COG2319   333 SLSFSPdgsllvsggsddgtirlwdLRTGKPLKTLEGHSNVLSVSFSPDGRVVSSGSTDGTVRLWDLSTGSLLRNLDGHT 412
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767912070 3713 SPVTAVSASETSGDIATVCDSagggSDLRLWTVNGDL 3749
Cdd:COG2319   413 SRVTSLDFSPDGKSLASGSSD----NTIRLWDLKTSL 445
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
3666-3698 1.97e-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: 1.97e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 767912070   3666 LYGHTEEITSLFVCKPYSILISVSRDGTCIIWD 3698
Cdd:smart00320    8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
3666-3698 1.94e-03

WD domain, G-beta repeat;


Pssm-ID: 425662 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 1.94e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767912070  3666 LYGHTEEITSLFVCKPYSILISVSRDGTCIIWD 3698
Cdd:pfam00400    7 LEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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