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Conserved domains on  [gi|1387248087|ref|XP_005226638|]
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WD repeat- and FYVE domain-containing protein 4 isoform X3 [Bos taurus]

Protein Classification

PH and BEACH domain-containing protein( domain architecture ID 12912966)

PH (Pleckstrin Homology) and Beige and Chediak Higashi (BEACH) domain-containing protein with WD40 repeat(s), such as WD repeat- and FYVE domain-containing protein 4 (WDFY4) that plays a role in the regulation of cDC1-mediated cross-presentation of viral and tumor antigens in dendritic cells; may be involved in facilitating membrane-dependent cellular processes

CATH:  2.30.29.30|2.130.10.10
Gene Ontology:  GO:0005515
PubMed:  12234919|23521701|15493994|22728242|14594214|30069656|29026209|21468892
SCOP:  4002395|4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Beach pfam02138
Beige/BEACH domain;
2543-2824 1.82e-177

Beige/BEACH domain;


:

Pssm-ID: 460459  Cd Length: 277  Bit Score: 545.53  E-value: 1.82e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2543 QKWQKRDISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSQTLNLMNPKTFRDLSKPMGAQTKERKLKFIQRFKEVE 2622
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2623 ktegDVTARCHYCTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKNAWESASrENMSDVRELTPEFFYLP 2702
Cdd:pfam02138   81 ----DDDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKELIPEFFYLP 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2703 EFLTNCNALEFGCMQDGTALGDVQLPPWADGDPRKFISLHRQALESDFVSANLHHWIDLIFGYKQQGSAAVEAVNTFHPY 2782
Cdd:pfam02138  156 EFLLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPL 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1387248087 2783 FYGDKVDLSSISDPLIRSTILGFVSNFGQVPKQLFTKPHPAR 2824
Cdd:pfam02138  236 TYEGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2391-2515 1.65e-23

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: 97.69  E-value: 1.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2391 EKVTQKYSVVIVQGHLVCEGLLLFGQQHLYICENFTLSPVGDVyctrhclsnisdpfIFNMCSKDRSSDHYSCQRHSYGD 2470
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKI--------------VVINSQKVLSYKEHLVFKWSLSD 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1387248087 2471 LRELRQARFLLQDIALEVFFQNGYSKFLVFHNSDRSKVFKSFCSF 2515
Cdd:cd01201     67 IREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDVYKKLLSL 111
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2924-3185 1.20e-21

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: 98.18  E-value: 1.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2924 SDKILVTFENLAAWGRClCAACPSPTTIITAGTSAVVCVWELSMTKGRATglrlkqaLYGHTQAVTCLAASVTFSLLVSG 3003
Cdd:cd00200     40 TGELLRTLKGHTGPVRD-VAASADGTYLASGSSDKTIRLWDLETGECVRT-------LTGHTSYVSSVAFSPDGRILSSS 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3004 SQDRTCILWDLDHLTHVARLPAHRDGVSAVAISDVSGTIVSCAGAH-LSLWDV-NGQPLASITtawGPEGAITCCyvveg 3081
Cdd:cd00200    112 SRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGtIKLWDLrTGKCVATLT---GHTGEVNSV----- 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3082 pAWD-TSHVIITGSRDGMVRIWKTEDVKMSVPGQAAPEEPWapsspSPRVHRWEKNLALCRElDVSVAL----TGKPSKA 3156
Cdd:cd00200    184 -AFSpDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVN-----SVAFSPDGYLLASGSE-DGTIRVwdlrTGECVQT 256

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1387248087 3157 ----NSAVTALAVSRNQTKLLVGDEKGRIFCWS 3185
Cdd:cd00200    257 lsghTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
 
Name Accession Description Interval E-value
Beach pfam02138
Beige/BEACH domain;
2543-2824 1.82e-177

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 545.53  E-value: 1.82e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2543 QKWQKRDISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSQTLNLMNPKTFRDLSKPMGAQTKERKLKFIQRFKEVE 2622
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2623 ktegDVTARCHYCTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKNAWESASrENMSDVRELTPEFFYLP 2702
Cdd:pfam02138   81 ----DDDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKELIPEFFYLP 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2703 EFLTNCNALEFGCMQDGTALGDVQLPPWADGDPRKFISLHRQALESDFVSANLHHWIDLIFGYKQQGSAAVEAVNTFHPY 2782
Cdd:pfam02138  156 EFLLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPL 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1387248087 2783 FYGDKVDLSSISDPLIRSTILGFVSNFGQVPKQLFTKPHPAR 2824
Cdd:pfam02138  236 TYEGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 2543-2824 6.49e-170

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: 524.10  E-value: 6.49e-170
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087  2543 QKWQKRDISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSQTLNLMNPKTFRDLSKPMGAQTKERKLKFIQRFKEVE 2622
Cdd:smart01026    2 QKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEELE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087  2623 KtegDVTARCHYCTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKNAWESASRENMSDVRELTPEFFYLP 2702
Cdd:smart01026   82 D---PDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVKELIPEFFYLP 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087  2703 EFLTNCNALEFGCMQDGTALGDVQLPPWADGDPRKFISLHRQALESDFVSANLHHWIDLIFGYKQQGSAAVEAVNTFHPY 2782
Cdd:smart01026  159 EFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFHPL 238

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1387248087  2783 FYGDKVDLSSISDPLIRSTILGFVSNFGQVPKQLFTKPHPAR 2824
Cdd:smart01026  239 TYEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 2543-2824 3.82e-144

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: 450.16  E-value: 3.82e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2543 QKWQKRDISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSQTLNLMNPKTFRDLSKPMGAQTKERKLKFIQRFKEVE 2622
Cdd:cd06071      2 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERYESDS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2623 KTEGDvtaRCHYCTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKNAWESASrENMSDVRELTPEFFYLP 2702
Cdd:cd06071     82 DDSDP---PFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSAS-ENPSDVKELIPEFYYLP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2703 EFLTNCNALEFGCmQDGTALGDVQLPPWADGdPRKFISLHRQALESDFVSANLHHWIDLIFGYKQQGSAAVEAVNTFHPY 2782
Cdd:cd06071    158 EFFLNINKFDFGK-QDGEKVNDVELPPWAKS-PEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFHPL 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1387248087 2783 FYGDKVDLSSISdpLIRSTILGFVSNFGQVPKQLFTKPHPAR 2824
Cdd:cd06071    236 TYEGSVDLDSID--VEREAIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2391-2515 1.65e-23

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: 97.69  E-value: 1.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2391 EKVTQKYSVVIVQGHLVCEGLLLFGQQHLYICENFTLSPVGDVyctrhclsnisdpfIFNMCSKDRSSDHYSCQRHSYGD 2470
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKI--------------VVINSQKVLSYKEHLVFKWSLSD 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1387248087 2471 LRELRQARFLLQDIALEVFFQNGYSKFLVFHNSDRSKVFKSFCSF 2515
Cdd:cd01201     67 IREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDVYKKLLSL 111
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2924-3185 1.20e-21

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: 98.18  E-value: 1.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2924 SDKILVTFENLAAWGRClCAACPSPTTIITAGTSAVVCVWELSMTKGRATglrlkqaLYGHTQAVTCLAASVTFSLLVSG 3003
Cdd:cd00200     40 TGELLRTLKGHTGPVRD-VAASADGTYLASGSSDKTIRLWDLETGECVRT-------LTGHTSYVSSVAFSPDGRILSSS 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3004 SQDRTCILWDLDHLTHVARLPAHRDGVSAVAISDVSGTIVSCAGAH-LSLWDV-NGQPLASITtawGPEGAITCCyvveg 3081
Cdd:cd00200    112 SRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGtIKLWDLrTGKCVATLT---GHTGEVNSV----- 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3082 pAWD-TSHVIITGSRDGMVRIWKTEDVKMSVPGQAAPEEPWapsspSPRVHRWEKNLALCRElDVSVAL----TGKPSKA 3156
Cdd:cd00200    184 -AFSpDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVN-----SVAFSPDGYLLASGSE-DGTIRVwdlrTGECVQT 256

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1387248087 3157 ----NSAVTALAVSRNQTKLLVGDEKGRIFCWS 3185
Cdd:cd00200    257 lsghTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
2947-3188 1.45e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 100.37  E-value: 1.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2947 SP--TTIITAGTSAVVCVWELsmtkgrATGlRLKQALYGHTQAVTCLAasvtFS----LLVSGSQDRTCILWDLDHLTHV 3020
Cdd:COG2319    129 SPdgKTLASGSADGTVRLWDL------ATG-KLLRTLTGHSGAVTSVA----FSpdgkLLASGSDDGTVRLWDLATGKLL 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3021 ARLPAHRDGVSAVAISDVSGTIVSCAGAH-LSLWDVN-GQPLASITtawGPEGAITCCyvvegpAWDT-SHVIITGSRDG 3097
Cdd:COG2319    198 RTLTGHTGAVRSVAFSPDGKLLASGSADGtVRLWDLAtGKLLRTLT---GHSGSVRSV------AFSPdGRLLASGSADG 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3098 MVRIWKTEDVKMSVPGQAAPEEPWA----P-------SSPSPRVHRWekNLALCRELDVsvaLTGKpskaNSAVTALAVS 3166
Cdd:COG2319    269 TVRLWDLATGELLRTLTGHSGGVNSvafsPdgkllasGSDDGTVRLW--DLATGKLLRT---LTGH----TGAVRSVAFS 339

                          250       260
                   ....*....|....*....|..
gi 1387248087 3167 RNQTKLLVGDEKGRIFCWSAEG 3188
Cdd:COG2319    340 PDGKTLASGSDDGTVRLWDLAT 361
WD40 pfam00400
WD domain, G-beta repeat;
2976-3013 2.14e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 2.14e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1387248087 2976 RLKQALYGHTQAVTCLAASVTFSLLVSGSQDRTCILWD 3013
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 2976-3013 6.16e-06

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: 45.38  E-value: 6.16e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1387248087  2976 RLKQALYGHTQAVTCLAASVTFSLLVSGSQDRTCILWD 3013
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 2467-2511 1.70e-04

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: 43.02  E-value: 1.70e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1387248087 2467 SYGDLRELRQARFLLQDIALEVFFQNGYSKFLVF-HNSDRSKVFKS 2511
Cdd:pfam14844   52 PISDIKEVHLRRYLLRDTALEIFLIDRTSLFFNFpDTGTRRKVYRK 97
 
Name Accession Description Interval E-value
Beach pfam02138
Beige/BEACH domain;
2543-2824 1.82e-177

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 545.53  E-value: 1.82e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2543 QKWQKRDISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSQTLNLMNPKTFRDLSKPMGAQTKERKLKFIQRFKEVE 2622
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2623 ktegDVTARCHYCTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKNAWESASrENMSDVRELTPEFFYLP 2702
Cdd:pfam02138   81 ----DDDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKELIPEFFYLP 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2703 EFLTNCNALEFGCMQDGTALGDVQLPPWADGDPRKFISLHRQALESDFVSANLHHWIDLIFGYKQQGSAAVEAVNTFHPY 2782
Cdd:pfam02138  156 EFLLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPL 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1387248087 2783 FYGDKVDLSSISDPLIRSTILGFVSNFGQVPKQLFTKPHPAR 2824
Cdd:pfam02138  236 TYEGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 2543-2824 6.49e-170

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: 524.10  E-value: 6.49e-170
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087  2543 QKWQKRDISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSQTLNLMNPKTFRDLSKPMGAQTKERKLKFIQRFKEVE 2622
Cdd:smart01026    2 QKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEELE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087  2623 KtegDVTARCHYCTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKNAWESASRENMSDVRELTPEFFYLP 2702
Cdd:smart01026   82 D---PDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVKELIPEFFYLP 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087  2703 EFLTNCNALEFGCMQDGTALGDVQLPPWADGDPRKFISLHRQALESDFVSANLHHWIDLIFGYKQQGSAAVEAVNTFHPY 2782
Cdd:smart01026  159 EFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFHPL 238

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1387248087  2783 FYGDKVDLSSISDPLIRSTILGFVSNFGQVPKQLFTKPHPAR 2824
Cdd:smart01026  239 TYEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 2543-2824 3.82e-144

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: 450.16  E-value: 3.82e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2543 QKWQKRDISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSQTLNLMNPKTFRDLSKPMGAQTKERKLKFIQRFKEVE 2622
Cdd:cd06071      2 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERYESDS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2623 KTEGDvtaRCHYCTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKNAWESASrENMSDVRELTPEFFYLP 2702
Cdd:cd06071     82 DDSDP---PFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSAS-ENPSDVKELIPEFYYLP 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2703 EFLTNCNALEFGCmQDGTALGDVQLPPWADGdPRKFISLHRQALESDFVSANLHHWIDLIFGYKQQGSAAVEAVNTFHPY 2782
Cdd:cd06071    158 EFFLNINKFDFGK-QDGEKVNDVELPPWAKS-PEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFHPL 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1387248087 2783 FYGDKVDLSSISdpLIRSTILGFVSNFGQVPKQLFTKPHPAR 2824
Cdd:cd06071    236 TYEGSVDLDSID--VEREAIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2391-2515 1.65e-23

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: 97.69  E-value: 1.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2391 EKVTQKYSVVIVQGHLVCEGLLLFGQQHLYICENFTLSPVGDVyctrhclsnisdpfIFNMCSKDRSSDHYSCQRHSYGD 2470
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKI--------------VVINSQKVLSYKEHLVFKWSLSD 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1387248087 2471 LRELRQARFLLQDIALEVFFQNGYSKFLVFHNSDRSKVFKSFCSF 2515
Cdd:cd01201     67 IREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDVYKKLLSL 111
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2924-3185 1.20e-21

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: 98.18  E-value: 1.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2924 SDKILVTFENLAAWGRClCAACPSPTTIITAGTSAVVCVWELSMTKGRATglrlkqaLYGHTQAVTCLAASVTFSLLVSG 3003
Cdd:cd00200     40 TGELLRTLKGHTGPVRD-VAASADGTYLASGSSDKTIRLWDLETGECVRT-------LTGHTSYVSSVAFSPDGRILSSS 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3004 SQDRTCILWDLDHLTHVARLPAHRDGVSAVAISDVSGTIVSCAGAH-LSLWDV-NGQPLASITtawGPEGAITCCyvveg 3081
Cdd:cd00200    112 SRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGtIKLWDLrTGKCVATLT---GHTGEVNSV----- 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3082 pAWD-TSHVIITGSRDGMVRIWKTEDVKMSVPGQAAPEEPWapsspSPRVHRWEKNLALCRElDVSVAL----TGKPSKA 3156
Cdd:cd00200    184 -AFSpDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVN-----SVAFSPDGYLLASGSE-DGTIRVwdlrTGECVQT 256

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1387248087 3157 ----NSAVTALAVSRNQTKLLVGDEKGRIFCWS 3185
Cdd:cd00200    257 lsghTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
2947-3188 1.45e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 100.37  E-value: 1.45e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2947 SP--TTIITAGTSAVVCVWELsmtkgrATGlRLKQALYGHTQAVTCLAasvtFS----LLVSGSQDRTCILWDLDHLTHV 3020
Cdd:COG2319    129 SPdgKTLASGSADGTVRLWDL------ATG-KLLRTLTGHSGAVTSVA----FSpdgkLLASGSDDGTVRLWDLATGKLL 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3021 ARLPAHRDGVSAVAISDVSGTIVSCAGAH-LSLWDVN-GQPLASITtawGPEGAITCCyvvegpAWDT-SHVIITGSRDG 3097
Cdd:COG2319    198 RTLTGHTGAVRSVAFSPDGKLLASGSADGtVRLWDLAtGKLLRTLT---GHSGSVRSV------AFSPdGRLLASGSADG 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3098 MVRIWKTEDVKMSVPGQAAPEEPWA----P-------SSPSPRVHRWekNLALCRELDVsvaLTGKpskaNSAVTALAVS 3166
Cdd:COG2319    269 TVRLWDLATGELLRTLTGHSGGVNSvafsPdgkllasGSDDGTVRLW--DLATGKLLRT---LTGH----TGAVRSVAFS 339

                          250       260
                   ....*....|....*....|..
gi 1387248087 3167 RNQTKLLVGDEKGRIFCWSAEG 3188
Cdd:COG2319    340 PDGKTLASGSDDGTVRLWDLAT 361
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2977-3108 2.29e-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: 94.32  E-value: 2.29e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2977 LKQALYGHTQAVTCLAASVTFSLLVSGSQDRTCILWDLDHLTHVARLPAHRDGVSAVAISDVSGTIVSCAGAH-LSLWDV 3055
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKtIRLWDL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1387248087 3056 NGQPLASITTawGPEGAITCCyvvegpAW-DTSHVIITGSRDGMVRIWKTEDVK 3108
Cdd:cd00200     81 ETGECVRTLT--GHTSYVSSV------AFsPDGRILSSSSRDKTIKVWDVETGK 126
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2936-3102 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 1387248087 2936 AWGRCLCAAcPSPTTIITAGTSAVVCVWELsmtkgraTGLRLKQALYGHTQAVTCLAASVTFSLLVSGSQDRTCILWDLD 3015
Cdd:cd00200     10 GGVTCVAFS-PDGKLLATGSGDGTIKVWDL-------ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3016 HLTHVARLPAHRDGVSAVAISDvSGTIVSCAGAHLS--LWDV-NGQPLASITtawGPEGAITCCyvvegpAWD-TSHVII 3091
Cdd:cd00200     82 TGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKTikVWDVeTGKCLTTLR---GHTDWVNSV------AFSpDGTFVA 151

                          170
                   ....*....|.
gi 1387248087 3092 TGSRDGMVRIW 3102
Cdd:cd00200    152 SSSQDGTIKLW 162
WD40 COG2319
WD40 repeat [General function prediction only];
2947-3106 1.82e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 93.82  E-value: 1.82e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2947 SP--TTIITAGTSAVVCVWELsmtkgrATGlRLKQALYGHTQAVTclaaSVTFS----LLVSGSQDRTCILWDLDHLTHV 3020
Cdd:COG2319    255 SPdgRLLASGSADGTVRLWDL------ATG-ELLRTLTGHSGGVN----SVAFSpdgkLLASGSDDGTVRLWDLATGKLL 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3021 ARLPAHRDGVSAVAISDVSGTIVS-CAGAHLSLWDVNGQPLasITTAWGPEGAITCCyvvegpAWD-TSHVIITGSRDGM 3098
Cdd:COG2319    324 RTLTGHTGAVRSVAFSPDGKTLASgSDDGTVRLWDLATGEL--LRTLTGHTGAVTSV------AFSpDGRTLASGSADGT 395


                   ....*...
gi 1387248087 3099 VRIWKTED 3106
Cdd:COG2319    396 VRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
2924-3188 6.33e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 92.28  E-value: 6.33e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2924 SDKILVTFENLAAWGRCLcAACPSPTTIITAGTSAVVCVWELsmtkgrATGlRLKQALYGHTQAVTCLAASVTFSLLVSG 3003
Cdd:COG2319    193 TGKLLRTLTGHTGAVRSV-AFSPDGKLLASGSADGTVRLWDL------ATG-KLLRTLTGHSGSVRSVAFSPDGRLLASG 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3004 SQDRTCILWDLDHLTHVARLPAHRDGVSAVAISDVSGTIVS-CAGAHLSLWDVN-GQPLASITtawGPEGAITCCyvveg 3081
Cdd:COG2319    265 SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASgSDDGTVRLWDLAtGKLLRTLT---GHTGAVRSV----- 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3082 pAW-DTSHVIITGSRDGMVRIWKTEDVKmsvpgqaapeepwapsspsprvhrweknlalcreldVSVALTGkpskANSAV 3160
Cdd:COG2319    337 -AFsPDGKTLASGSDDGTVRLWDLATGE------------------------------------LLRTLTG----HTGAV 375

                          250       260
                   ....*....|....*....|....*...
gi 1387248087 3161 TALAVSRNQTKLLVGDEKGRIFCWSAEG 3188
Cdd:COG2319    376 TSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
2941-3188 2.54e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 87.27  E-value: 2.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2941 LCAACPSPTTIITAGTSAVVCVWelsmtkgRATGLRLKQALYGHTQAVTCLAASVTFSLLVSGSQDRTCILWDLDHLTHV 3020
Cdd:COG2319     41 SLAASPDGARLAAGAGDLTLLLL-------DAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLL 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3021 ARLPAHRDGVSAVAISDVSGTIVSCAGAH-LSLWDV-NGQPLASITtawGPEGAITCCyvvegpAWD-TSHVIITGSRDG 3097
Cdd:COG2319    114 RTLTGHTGAVRSVAFSPDGKTLASGSADGtVRLWDLaTGKLLRTLT---GHSGAVTSV------AFSpDGKLLASGSDDG 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 3098 MVRIWKTEDVKMSVPGQAAPEEPWAPS-SPSPR----------VHRWekNLALCRELDVsvaLTGKpskaNSAVTALAVS 3166
Cdd:COG2319    185 TVRLWDLATGKLLRTLTGHTGAVRSVAfSPDGKllasgsadgtVRLW--DLATGKLLRT---LTGH----SGSVRSVAFS 255

                          250       260
                   ....*....|....*....|..
gi 1387248087 3167 RNQTKLLVGDEKGRIFCWSAEG 3188
Cdd:COG2319    256 PDGRLLASGSADGTVRLWDLAT 277
WD40 pfam00400
WD domain, G-beta repeat;
2976-3013 2.14e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.57  E-value: 2.14e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1387248087 2976 RLKQALYGHTQAVTCLAASVTFSLLVSGSQDRTCILWD 3013
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 2976-3013 6.16e-06

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: 45.38  E-value: 6.16e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1387248087  2976 RLKQALYGHTQAVTCLAASVTFSLLVSGSQDRTCILWD 3013
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 2942-3062 8.89e-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: 50.84  E-value: 8.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387248087 2942 CAACPSPTTIITAGT-SAVVCVWELSmtKGRATGLRLKQA------------------LYGHTQAVTCLAASVTFSLLVS 3002
Cdd:pfam20426  129 CVAVTSDGSILATGSyDTTVMVWEVL--RGRSSEKRSRNTqtefprkdhviaetpfhiLCGHDDIITCLYVSVELDIVIS 206

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387248087 3003 GSQDRTCILWDLDHLTHV--ARLPaHRDGVSAVAISDvSGTIVSCAGAHLSL--WDVNGQPLAS 3062
Cdd:pfam20426  207 GSKDGTCIFHTLREGRYVrsIRHP-SGCPLSKLVASR-HGRIVLYADDDLSLhlYSINGKHIAS 268
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 2467-2511 1.70e-04

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: 43.02  E-value: 1.70e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1387248087 2467 SYGDLRELRQARFLLQDIALEVFFQNGYSKFLVF-HNSDRSKVFKS 2511
Cdd:pfam14844   52 PISDIKEVHLRRYLLRDTALEIFLIDRTSLFFNFpDTGTRRKVYRK 97
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3056-3103 7.52e-03

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: 36.52  E-value: 7.52e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*....
gi 1387248087  3056 NGQPLASITtawGPEGAITCCyvvegpAWD-TSHVIITGSRDGMVRIWK 3103
Cdd:smart00320    1 SGELLKTLK---GHTGPVTSV------AFSpDGKYLASGSDDGTIKLWD 40
 
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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