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Conserved domains on  [gi|1034568988|ref|XP_016871952|]
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WD repeat- and FYVE domain-containing protein 4 isoform X1 [Homo sapiens]

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;
2540-2821 2.16e-175

Beige/BEACH domain;


:

Pssm-ID: 460459  Cd Length: 277  Bit Score: 539.75  E-value: 2.16e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2540 QKWQKRDISNFEYLMYLNTAAGRTCNDYMQYPVFPWVLADYTSETLNLANPKIFRDLSKPMGAQTKERKLKFIQRFKEVE 2619
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2620 ktegDMTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCALQGGSFDVADRMFHSVKSTWESASrENMSDVRELTPEFFYLP 2699
Cdd:pfam02138   81 ----DDDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKELIPEFFYLP 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2700 EFLTNCNGVEFGCMQDGTVLGDVQLPPWADGDPRKFISLHRKALESDFVSANLHHWIDLIFGYKQQGPAAVDAVNIFHPY 2779
Cdd:pfam02138  156 EFLLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPL 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1034568988 2780 FYGDRMDLSSITDPLIKSTILGFVSNFGQVPKQLFTKPHPAR 2821
Cdd:pfam02138  236 TYEGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2902-3100 2.24e-22

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: 100.10  E-value: 2.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2902 NRTFSWGFDDFSCCLGSYGSDKVLMTFENLAAWGRClCAVCPSPTTIVTSGTSTVVCVWELsmtkgrpRGLRLRQALYGH 2981
Cdd:cd00200    105 GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS-VAFSPDGTFVASSSQDGTIKLWDL-------RTGKCVATLTGH 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2982 TQAVTCLAASVTFSLLVSGSQDCTCILWDLDHLTHVTRLPAHREGISAITISDVSGTIVSCAGA-HLSLWNV-NGQPLAS 3059
Cdd:cd00200    177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDgTIRVWDLrTGECVQT 256

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1034568988 3060 ITtawGPEGAITCCclmegpAWD-TSQIIITGSQDGMVRVWK 3100
Cdd:cd00200    257 LS---GHTNSVTSL------AWSpDGKRLASGSADGTIRIWD 289
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2388-2512 3.38e-19

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: 85.36  E-value: 3.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2388 EKVTQKFSLVIVQGHLVSEGVLLFGHQHFYICENFTLSPTGDVYCTRhclsnisdpfifnlCSKDRSTDHYSCQCHSYAD 2467
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVVIN--------------SQKVLSYKEHLVFKWSLSD 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034568988 2468 MRELRQARFLLQDIALEIFFHNGYSKFLVFYNNDRSKAFKSFCSF 2512
Cdd:cd01201     67 IREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDVYKKLLSL 111
 
Name Accession Description Interval E-value
Beach pfam02138
Beige/BEACH domain;
2540-2821 2.16e-175

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 539.75  E-value: 2.16e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2540 QKWQKRDISNFEYLMYLNTAAGRTCNDYMQYPVFPWVLADYTSETLNLANPKIFRDLSKPMGAQTKERKLKFIQRFKEVE 2619
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2620 ktegDMTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCALQGGSFDVADRMFHSVKSTWESASrENMSDVRELTPEFFYLP 2699
Cdd:pfam02138   81 ----DDDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKELIPEFFYLP 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2700 EFLTNCNGVEFGCMQDGTVLGDVQLPPWADGDPRKFISLHRKALESDFVSANLHHWIDLIFGYKQQGPAAVDAVNIFHPY 2779
Cdd:pfam02138  156 EFLLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPL 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1034568988 2780 FYGDRMDLSSITDPLIKSTILGFVSNFGQVPKQLFTKPHPAR 2821
Cdd:pfam02138  236 TYEGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 2540-2821 3.30e-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: 524.87  E-value: 3.30e-170
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988  2540 QKWQKRDISNFEYLMYLNTAAGRTCNDYMQYPVFPWVLADYTSETLNLANPKIFRDLSKPMGAQTKERKLKFIQRFKEVE 2619
Cdd:smart01026    2 QKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEELE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988  2620 KTEgdmTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCALQGGSFDVADRMFHSVKSTWESASRENMSDVRELTPEFFYLP 2699
Cdd:smart01026   82 DPD---IPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVKELIPEFFYLP 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988  2700 EFLTNCNGVEFGCMQDGTVLGDVQLPPWADGDPRKFISLHRKALESDFVSANLHHWIDLIFGYKQQGPAAVDAVNIFHPY 2779
Cdd:smart01026  159 EFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFHPL 238

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1034568988  2780 FYGDRMDLSSITDPLIKSTILGFVSNFGQVPKQLFTKPHPAR 2821
Cdd:smart01026  239 TYEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 2540-2821 2.36e-141

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: 442.07  E-value: 2.36e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2540 QKWQKRDISNFEYLMYLNTAAGRTCNDYMQYPVFPWVLADYTSETLNLANPKIFRDLSKPMGAQTKERKlkfiQRFKEVE 2619
Cdd:cd06071      2 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERL----QLLKERY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2620 KTEGDMTVQ-CHYYTHYSSAIIVASYLVRMPPFTQAFCALQGGSFDVADRMFHSVKSTWESASrENMSDVRELTPEFFYL 2698
Cdd:cd06071     78 ESDSDDSDPpFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSAS-ENPSDVKELIPEFYYL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2699 PEFLTNCNGVEFGCmQDGTVLGDVQLPPWADGdPRKFISLHRKALESDFVSANLHHWIDLIFGYKQQGPAAVDAVNIFHP 2778
Cdd:cd06071    157 PEFFLNINKFDFGK-QDGEKVNDVELPPWAKS-PEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFHP 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1034568988 2779 YFYGDRMDLSSITdpLIKSTILGFVSNFGQVPKQLFTKPHPAR 2821
Cdd:cd06071    235 LTYEGSVDLDSID--VEREAIEAQINNFGQTPVQLFTKPHPKR 275
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2902-3100 2.24e-22

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: 100.10  E-value: 2.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2902 NRTFSWGFDDFSCCLGSYGSDKVLMTFENLAAWGRClCAVCPSPTTIVTSGTSTVVCVWELsmtkgrpRGLRLRQALYGH 2981
Cdd:cd00200    105 GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS-VAFSPDGTFVASSSQDGTIKLWDL-------RTGKCVATLTGH 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2982 TQAVTCLAASVTFSLLVSGSQDCTCILWDLDHLTHVTRLPAHREGISAITISDVSGTIVSCAGA-HLSLWNV-NGQPLAS 3059
Cdd:cd00200    177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDgTIRVWDLrTGECVQT 256

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1034568988 3060 ITtawGPEGAITCCclmegpAWD-TSQIIITGSQDGMVRVWK 3100
Cdd:cd00200    257 LS---GHTNSVTSL------AWSpDGKRLASGSADGTIRIWD 289
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2388-2512 3.38e-19

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: 85.36  E-value: 3.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2388 EKVTQKFSLVIVQGHLVSEGVLLFGHQHFYICENFTLSPTGDVYCTRhclsnisdpfifnlCSKDRSTDHYSCQCHSYAD 2467
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVVIN--------------SQKVLSYKEHLVFKWSLSD 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034568988 2468 MRELRQARFLLQDIALEIFFHNGYSKFLVFYNNDRSKAFKSFCSF 2512
Cdd:cd01201     67 IREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDVYKKLLSL 111
WD40 COG2319
WD40 repeat [General function prediction only];
2940-3184 8.00e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.90  E-value: 8.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2940 AVCPSP--TTIVTSGTSTVVCVWELsmtkgrpRGLRLRQALYGHTQAVTCLAasvtFS----LLVSGSQDCTCILWDLDH 3013
Cdd:COG2319    125 SVAFSPdgKTLASGSADGTVRLWDL-------ATGKLLRTLTGHSGAVTSVA----FSpdgkLLASGSDDGTVRLWDLAT 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3014 LTHVTRLPAHREGISAITISDVSGTIVSCAGAH-LSLWNVN-GQPLASITtawGPEGAITCCclmegpAWDT-SQIIITG 3090
Cdd:COG2319    194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGtVRLWDLAtGKLLRTLT---GHSGSVRSV------AFSPdGRLLASG 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3091 SQDGMVRVWKTEDvkmsvpGRPAGEEPPAQPP------SPRGhkweKNLALSRElDVSIAL----TGKPSKT----SPAV 3156
Cdd:COG2319    265 SADGTVRLWDLAT------GELLRTLTGHSGGvnsvafSPDG----KLLASGSD-DGTVRLwdlaTGKLLRTltghTGAV 333

                          250       260
                   ....*....|....*....|....*...
gi 1034568988 3157 TALAVSRNHTKLLVGDERGRIFCWSADG 3184
Cdd:COG2319    334 RSVAFSPDGKTLASGSDDGTVRLWDLAT 361
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 2940-3059 4.00e-07

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: 55.08  E-value: 4.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2940 AVCPSPTTIVTSGTSTVVCVWELSMTKGRPRGLRLRQA----------------LYGHTQAVTCLAASVTFSLLVSGSQD 3003
Cdd:pfam20426  131 AVTSDGSILATGSYDTTVMVWEVLRGRSSEKRSRNTQTefprkdhviaetpfhiLCGHDDIITCLYVSVELDIVISGSKD 210

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3004 CTCILWDLDHLTHV--TRLPaHREGISAITISDvSGTIVSCAGAHLSL--WNVNGQPLAS 3059
Cdd:pfam20426  211 GTCIFHTLREGRYVrsIRHP-SGCPLSKLVASR-HGRIVLYADDDLSLhlYSINGKHIAS 268
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 2973-3010 1.20e-05

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: 44.61  E-value: 1.20e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1034568988  2973 RLRQALYGHTQAVTCLAASVTFSLLVSGSQDCTCILWD 3010
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 2464-2508 6.98e-05

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: 44.18  E-value: 6.98e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1034568988 2464 SYADMRELRQARFLLQDIALEIFFHNGYSKFLVFYN-NDRSKAFKS 2508
Cdd:pfam14844   52 PISDIKEVHLRRYLLRDTALEIFLIDRTSLFFNFPDtGTRRKVYRK 97
 
Name Accession Description Interval E-value
Beach pfam02138
Beige/BEACH domain;
2540-2821 2.16e-175

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 539.75  E-value: 2.16e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2540 QKWQKRDISNFEYLMYLNTAAGRTCNDYMQYPVFPWVLADYTSETLNLANPKIFRDLSKPMGAQTKERKLKFIQRFKEVE 2619
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2620 ktegDMTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCALQGGSFDVADRMFHSVKSTWESASrENMSDVRELTPEFFYLP 2699
Cdd:pfam02138   81 ----DDDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKELIPEFFYLP 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2700 EFLTNCNGVEFGCMQDGTVLGDVQLPPWADGDPRKFISLHRKALESDFVSANLHHWIDLIFGYKQQGPAAVDAVNIFHPY 2779
Cdd:pfam02138  156 EFLLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPL 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1034568988 2780 FYGDRMDLSSITDPLIKSTILGFVSNFGQVPKQLFTKPHPAR 2821
Cdd:pfam02138  236 TYEGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 2540-2821 3.30e-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: 524.87  E-value: 3.30e-170
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988  2540 QKWQKRDISNFEYLMYLNTAAGRTCNDYMQYPVFPWVLADYTSETLNLANPKIFRDLSKPMGAQTKERKLKFIQRFKEVE 2619
Cdd:smart01026    2 QKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEELE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988  2620 KTEgdmTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCALQGGSFDVADRMFHSVKSTWESASRENMSDVRELTPEFFYLP 2699
Cdd:smart01026   82 DPD---IPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVKELIPEFFYLP 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988  2700 EFLTNCNGVEFGCMQDGTVLGDVQLPPWADGDPRKFISLHRKALESDFVSANLHHWIDLIFGYKQQGPAAVDAVNIFHPY 2779
Cdd:smart01026  159 EFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFHPL 238

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1034568988  2780 FYGDRMDLSSITDPLIKSTILGFVSNFGQVPKQLFTKPHPAR 2821
Cdd:smart01026  239 TYEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 2540-2821 2.36e-141

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: 442.07  E-value: 2.36e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2540 QKWQKRDISNFEYLMYLNTAAGRTCNDYMQYPVFPWVLADYTSETLNLANPKIFRDLSKPMGAQTKERKlkfiQRFKEVE 2619
Cdd:cd06071      2 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERL----QLLKERY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2620 KTEGDMTVQ-CHYYTHYSSAIIVASYLVRMPPFTQAFCALQGGSFDVADRMFHSVKSTWESASrENMSDVRELTPEFFYL 2698
Cdd:cd06071     78 ESDSDDSDPpFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSAS-ENPSDVKELIPEFYYL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2699 PEFLTNCNGVEFGCmQDGTVLGDVQLPPWADGdPRKFISLHRKALESDFVSANLHHWIDLIFGYKQQGPAAVDAVNIFHP 2778
Cdd:cd06071    157 PEFFLNINKFDFGK-QDGEKVNDVELPPWAKS-PEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFHP 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1034568988 2779 YFYGDRMDLSSITdpLIKSTILGFVSNFGQVPKQLFTKPHPAR 2821
Cdd:cd06071    235 LTYEGSVDLDSID--VEREAIEAQINNFGQTPVQLFTKPHPKR 275
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2902-3100 2.24e-22

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: 100.10  E-value: 2.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2902 NRTFSWGFDDFSCCLGSYGSDKVLMTFENLAAWGRClCAVCPSPTTIVTSGTSTVVCVWELsmtkgrpRGLRLRQALYGH 2981
Cdd:cd00200    105 GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS-VAFSPDGTFVASSSQDGTIKLWDL-------RTGKCVATLTGH 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2982 TQAVTCLAASVTFSLLVSGSQDCTCILWDLDHLTHVTRLPAHREGISAITISDVSGTIVSCAGA-HLSLWNV-NGQPLAS 3059
Cdd:cd00200    177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDgTIRVWDLrTGECVQT 256

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1034568988 3060 ITtawGPEGAITCCclmegpAWD-TSQIIITGSQDGMVRVWK 3100
Cdd:cd00200    257 LS---GHTNSVTSL------AWSpDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2908-3110 1.97e-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: 1.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2908 GFDDFSCCLGSYGSDKVLMTFENLAAWGRClCAVCPSPTTIVTSGTSTVVCVWELSMTKgrprglrLRQALYGHTQAVTC 2987
Cdd:cd00200     69 GSSDKTIRLWDLETGECVRTLTGHTSYVSS-VAFSPDGRILSSSSRDKTIKVWDVETGK-------CLTTLRGHTDWVNS 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2988 LAASVTFSLLVSGSQDCTCILWDLDHLTHVTRLPAHREGISAITISDVSGTIVSCAG-AHLSLWNVNGQplASITTAWGP 3066
Cdd:cd00200    141 VAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTG--KCLGTLRGH 218

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034568988 3067 EGAITCCCLMegpawDTSQIIITGSQDGMVRVW--KTEDVKMSVPG 3110
Cdd:cd00200    219 ENGVNSVAFS-----PDGYLLASGSEDGTIRVWdlRTGECVQTLSG 259
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2921-3099 1.02e-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: 92.40  E-value: 1.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2921 SDKVLMTFENLAAWGRClCAVCPSPTTIVTSGTSTVVCVWELSmtkgrprGLRLRQALYGHTQAVTCLAASVTFSLLVSG 3000
Cdd:cd00200     40 TGELLRTLKGHTGPVRD-VAASADGTYLASGSSDKTIRLWDLE-------TGECVRTLTGHTSYVSSVAFSPDGRILSSS 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3001 SQDCTCILWDLDHLTHVTRLPAHREGISAITISDVSGTIVSCAGAH-LSLWNV-NGQPLASITtawGPEGAITCCCLMeg 3078
Cdd:cd00200    112 SRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGtIKLWDLrTGKCVATLT---GHTGEVNSVAFS-- 186

                          170       180
                   ....*....|....*....|.
gi 1034568988 3079 pawDTSQIIITGSQDGMVRVW 3099
Cdd:cd00200    187 ---PDGEKLLSSSSDGTIKLW 204
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2974-3105 1.42e-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: 92.01  E-value: 1.42e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2974 LRQALYGHTQAVTCLAASVTFSLLVSGSQDCTCILWDLDHLTHVTRLPAHREGISAITISDVSGTIVSCAGAH-LSLWNV 3052
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKtIRLWDL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034568988 3053 NGQPLASITTawGPEGAITCCCLMegpawDTSQIIITGSQDGMVRVWKTEDVK 3105
Cdd:cd00200     81 ETGECVRTLT--GHTSYVSSVAFS-----PDGRILSSSSRDKTIKVWDVETGK 126
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2388-2512 3.38e-19

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: 85.36  E-value: 3.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2388 EKVTQKFSLVIVQGHLVSEGVLLFGHQHFYICENFTLSPTGDVYCTRhclsnisdpfifnlCSKDRSTDHYSCQCHSYAD 2467
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVVIN--------------SQKVLSYKEHLVFKWSLSD 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034568988 2468 MRELRQARFLLQDIALEIFFHNGYSKFLVFYNNDRSKAFKSFCSF 2512
Cdd:cd01201     67 IREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDVYKKLLSL 111
WD40 COG2319
WD40 repeat [General function prediction only];
2940-3184 8.00e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.90  E-value: 8.00e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2940 AVCPSP--TTIVTSGTSTVVCVWELsmtkgrpRGLRLRQALYGHTQAVTCLAasvtFS----LLVSGSQDCTCILWDLDH 3013
Cdd:COG2319    125 SVAFSPdgKTLASGSADGTVRLWDL-------ATGKLLRTLTGHSGAVTSVA----FSpdgkLLASGSDDGTVRLWDLAT 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3014 LTHVTRLPAHREGISAITISDVSGTIVSCAGAH-LSLWNVN-GQPLASITtawGPEGAITCCclmegpAWDT-SQIIITG 3090
Cdd:COG2319    194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGtVRLWDLAtGKLLRTLT---GHSGSVRSV------AFSPdGRLLASG 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3091 SQDGMVRVWKTEDvkmsvpGRPAGEEPPAQPP------SPRGhkweKNLALSRElDVSIAL----TGKPSKT----SPAV 3156
Cdd:COG2319    265 SADGTVRLWDLAT------GELLRTLTGHSGGvnsvafSPDG----KLLASGSD-DGTVRLwdlaTGKLLRTltghTGAV 333

                          250       260
                   ....*....|....*....|....*...
gi 1034568988 3157 TALAVSRNHTKLLVGDERGRIFCWSADG 3184
Cdd:COG2319    334 RSVAFSPDGKTLASGSDDGTVRLWDLAT 361
WD40 COG2319
WD40 repeat [General function prediction only];
2921-3184 2.05e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 90.74  E-value: 2.05e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2921 SDKVLMTFENLAAWGRCLcAVCPSPTTIVTSGTSTVVCVWELsmtkgrpRGLRLRQALYGHTQAVTCLAASVTFSLLVSG 3000
Cdd:COG2319    193 TGKLLRTLTGHTGAVRSV-AFSPDGKLLASGSADGTVRLWDL-------ATGKLLRTLTGHSGSVRSVAFSPDGRLLASG 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3001 SQDCTCILWDLDHLTHVTRLPAHREGISAITISDVSGTIVS-CAGAHLSLWNVN-GQPLASITtawGPEGAITCCclmeg 3078
Cdd:COG2319    265 SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASgSDDGTVRLWDLAtGKLLRTLT---GHTGAVRSV----- 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3079 pAW-DTSQIIITGSQDGMVRVWKTEDVKmsvpgrpageeppaQPPSPRGHkweknlalsreldvsialtgkpsktSPAVT 3157
Cdd:COG2319    337 -AFsPDGKTLASGSDDGTVRLWDLATGE--------------LLRTLTGH-------------------------TGAVT 376

                          250       260
                   ....*....|....*....|....*..
gi 1034568988 3158 ALAVSRNHTKLLVGDERGRIFCWSADG 3184
Cdd:COG2319    377 SVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2933-3099 3.58e-17

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: 84.69  E-value: 3.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2933 AWGRCLCaVCPSPTTIVTSGTSTVVCVWELSmtkgrprGLRLRQALYGHTQAVTCLAASVTFSLLVSGSQDCTCILWDLD 3012
Cdd:cd00200     10 GGVTCVA-FSPDGKLLATGSGDGTIKVWDLE-------TGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3013 HLTHVTRLPAHREGISAITISDvSGTIVSCAGAHLS--LWNV-NGQPLASITtawGPEGAITCCclmegpAWD-TSQIII 3088
Cdd:cd00200     82 TGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKTikVWDVeTGKCLTTLR---GHTDWVNSV------AFSpDGTFVA 151

                          170
                   ....*....|.
gi 1034568988 3089 TGSQDGMVRVW 3099
Cdd:cd00200    152 SSSQDGTIKLW 162
WD40 COG2319
WD40 repeat [General function prediction only];
2943-3183 3.75e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 86.89  E-value: 3.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2943 PSPTTIVTSGTSTVVCVWELSmtkgrprGLRLRQALYGHTQAVTCLAASVTFSLLVSGSQDCTCILWDLDHLTHVTRLPA 3022
Cdd:COG2319     88 PDGRLLASASADGTVRLWDLA-------TGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTG 160

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3023 HREGISAITISDVSGTIVSCAGAH-LSLWNV-NGQPLASITtawGPEGAITCCclmegpAWD-TSQIIITGSQDGMVRVW 3099
Cdd:COG2319    161 HSGAVTSVAFSPDGKLLASGSDDGtVRLWDLaTGKLLRTLT---GHTGAVRSV------AFSpDGKLLASGSADGTVRLW 231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3100 KTEDVKmsVPGRPAGEEPPAQPP--SPRGHkweknLALSRELDVSIAL----TGKPSKT----SPAVTALAVSRNHTKLL 3169
Cdd:COG2319    232 DLATGK--LLRTLTGHSGSVRSVafSPDGR-----LLASGSADGTVRLwdlaTGELLRTltghSGGVNSVAFSPDGKLLA 304

                          250
                   ....*....|....
gi 1034568988 3170 VGDERGRIFCWSAD 3183
Cdd:COG2319    305 SGSDDGTVRLWDLA 318
WD40 COG2319
WD40 repeat [General function prediction only];
2968-3184 6.22e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 6.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2968 RPRGLRLRQALYGHTQAVTCLAASVTFSLLVSGSQDCTCILWDLDHLTHVTRLPAHREGISAITISDVSGTIVSCAGAH- 3046
Cdd:COG2319     64 DAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGt 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3047 LSLWNV-NGQPLASITtawGPEGAITCCclmegpAWD-TSQIIITGSQDGMVRVWKTEDvkmsvpGRPAGEEPPAQPP-- 3122
Cdd:COG2319    144 VRLWDLaTGKLLRTLT---GHSGAVTSV------AFSpDGKLLASGSDDGTVRLWDLAT------GKLLRTLTGHTGAvr 208

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034568988 3123 ----SPRGhkweKNLALSRElDVSIAL----TGKPSKT----SPAVTALAVSRNHTKLLVGDERGRIFCWSADG 3184
Cdd:COG2319    209 svafSPDG----KLLASGSA-DGTVRLwdlaTGKLLRTltghSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT 277
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 2940-3059 4.00e-07

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: 55.08  E-value: 4.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 2940 AVCPSPTTIVTSGTSTVVCVWELSMTKGRPRGLRLRQA----------------LYGHTQAVTCLAASVTFSLLVSGSQD 3003
Cdd:pfam20426  131 AVTSDGSILATGSYDTTVMVWEVLRGRSSEKRSRNTQTefprkdhviaetpfhiLCGHDDIITCLYVSVELDIVISGSKD 210

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034568988 3004 CTCILWDLDHLTHV--TRLPaHREGISAITISDvSGTIVSCAGAHLSL--WNVNGQPLAS 3059
Cdd:pfam20426  211 GTCIFHTLREGRYVrsIRHP-SGCPLSKLVASR-HGRIVLYADDDLSLhlYSINGKHIAS 268
WD40 pfam00400
WD domain, G-beta repeat;
2973-3010 4.09e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 4.09e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1034568988 2973 RLRQALYGHTQAVTCLAASVTFSLLVSGSQDCTCILWD 3010
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 2973-3010 1.20e-05

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: 44.61  E-value: 1.20e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1034568988  2973 RLRQALYGHTQAVTCLAASVTFSLLVSGSQDCTCILWD 3010
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 2464-2508 6.98e-05

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: 44.18  E-value: 6.98e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1034568988 2464 SYADMRELRQARFLLQDIALEIFFHNGYSKFLVFYN-NDRSKAFKS 2508
Cdd:pfam14844   52 PISDIKEVHLRRYLLRDTALEIFLIDRTSLFFNFPDtGTRRKVYRK 97
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 3053-3100 5.43e-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: 36.91  E-value: 5.43e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1034568988  3053 NGQPLASITtawGPEGAITCCCLMegpawDTSQIIITGSQDGMVRVWK 3100
Cdd:smart00320    1 SGELLKTLK---GHTGPVTSVAFS-----PDGKYLASGSDDGTIKLWD 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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