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Conserved domains on  [gi|1767181131|sp|E9Q2M9|]
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RecName: Full=WD repeat- and FYVE domain-containing protein 4

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;
2538-2819 8.13e-176

Beige/BEACH domain;


:

Pssm-ID: 460459  Cd Length: 277  Bit Score: 540.91  E-value: 8.13e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2538 QRWQKREISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSEMLNLTNPKTFRDLSKPMGAQTKERKLKFTQRFKDVE 2617
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2618 kiegDMTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKSTWESASkENMSDVRELTPEFFYLP 2697
Cdd:pfam02138   81 ----DDDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKELIPEFFYLP 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2698 EFLTNCNAVEFGCMQDGTTLGDVQLPPWADGDPRKFISLHRQALESDFVSSNLHHWIDLIFGYKQQGPAAVEAVNTFHPY 2777
Cdd:pfam02138  156 EFLLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPL 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1767181131 2778 FYGDRIDLGSITDPLIKSTILGFISNFGQVPKQIFTKPHPSR 2819
Cdd:pfam02138  236 TYEGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2386-2507 3.01e-22

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: 94.22  E-value: 3.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2386 EKVSQKVPMVIVQGHLVSEGILLFGQHHFYICENFTLSPTGDVycthhclsnisdpfIFNMCSKDRSSDHYSCQRHAYSD 2465
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKI--------------VVINSQKVLSYKEHLVFKWSLSD 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1767181131 2466 LRELRQARFLLQDIALEIFFQNGYSKLLVFYNSDRSKALKSF 2507
Cdd:cd01201     67 IREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDVYKKL 108
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2901-3099 5.13e-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: 98.95  E-value: 5.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2901 NRTFSWGFDDFSCCLGSYGSDKILMTFENLAAWGPClCAVCPSPTMIVTSGASAVVCIWELslvkgrpRGLKLRQALYGH 2980
Cdd:cd00200    105 GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS-VAFSPDGTFVASSSQDGTIKLWDL-------RTGKCVATLTGH 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2981 TQAVTCLTASVTFSLLVSGSQDRTCILWDLDHLSRVACLPVHREGISAIAISDVSGTIVSCAGA-HLSLWNV-NGQPLAS 3058
Cdd:cd00200    177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDgTIRVWDLrTGECVQT 256

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1767181131 3059 ITtawGPEGTITCCcivegpAWDAS-HVIITGSKDGMVRIWK 3099
Cdd:cd00200    257 LS---GHTNSVTSL------AWSPDgKRLASGSADGTIRIWD 289
 
Name Accession Description Interval E-value
Beach pfam02138
Beige/BEACH domain;
2538-2819 8.13e-176

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 540.91  E-value: 8.13e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2538 QRWQKREISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSEMLNLTNPKTFRDLSKPMGAQTKERKLKFTQRFKDVE 2617
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2618 kiegDMTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKSTWESASkENMSDVRELTPEFFYLP 2697
Cdd:pfam02138   81 ----DDDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKELIPEFFYLP 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2698 EFLTNCNAVEFGCMQDGTTLGDVQLPPWADGDPRKFISLHRQALESDFVSSNLHHWIDLIFGYKQQGPAAVEAVNTFHPY 2777
Cdd:pfam02138  156 EFLLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPL 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1767181131 2778 FYGDRIDLGSITDPLIKSTILGFISNFGQVPKQIFTKPHPSR 2819
Cdd:pfam02138  236 TYEGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 2538-2819 1.88e-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: 525.64  E-value: 1.88e-170
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131  2538 QRWQKREISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSEMLNLTNPKTFRDLSKPMGAQTKERKLKFTQRFKDVE 2617
Cdd:smart01026    2 QKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEELE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131  2618 KIEgdmTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKSTWESASKENMSDVRELTPEFFYLP 2697
Cdd:smart01026   82 DPD---IPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVKELIPEFFYLP 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131  2698 EFLTNCNAVEFGCMQDGTTLGDVQLPPWADGDPRKFISLHRQALESDFVSSNLHHWIDLIFGYKQQGPAAVEAVNTFHPY 2777
Cdd:smart01026  159 EFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFHPL 238

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1767181131  2778 FYGDRIDLGSITDPLIKSTILGFISNFGQVPKQIFTKPHPSR 2819
Cdd:smart01026  239 TYEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 2538-2819 4.24e-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: 449.77  E-value: 4.24e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2538 QRWQKREISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSEMLNLTNPKTFRDLSKPMGAQTKERKlkftQRFKDVE 2617
Cdd:cd06071      2 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERL----QLLKERY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2618 KIEGDMTVQ-CHYYTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKSTWESASkENMSDVRELTPEFFYL 2696
Cdd:cd06071     78 ESDSDDSDPpFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSAS-ENPSDVKELIPEFYYL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2697 PEFLTNCNAVEFGCmQDGTTLGDVQLPPWADGdPRKFISLHRQALESDFVSSNLHHWIDLIFGYKQQGPAAVEAVNTFHP 2776
Cdd:cd06071    157 PEFFLNINKFDFGK-QDGEKVNDVELPPWAKS-PEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFHP 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1767181131 2777 YFYGDRIDLGSITdpLIKSTILGFISNFGQVPKQIFTKPHPSR 2819
Cdd:cd06071    235 LTYEGSVDLDSID--VEREAIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2386-2507 3.01e-22

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: 94.22  E-value: 3.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2386 EKVSQKVPMVIVQGHLVSEGILLFGQHHFYICENFTLSPTGDVycthhclsnisdpfIFNMCSKDRSSDHYSCQRHAYSD 2465
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKI--------------VVINSQKVLSYKEHLVFKWSLSD 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1767181131 2466 LRELRQARFLLQDIALEIFFQNGYSKLLVFYNSDRSKALKSF 2507
Cdd:cd01201     67 IREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDVYKKL 108
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2901-3099 5.13e-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: 98.95  E-value: 5.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2901 NRTFSWGFDDFSCCLGSYGSDKILMTFENLAAWGPClCAVCPSPTMIVTSGASAVVCIWELslvkgrpRGLKLRQALYGH 2980
Cdd:cd00200    105 GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS-VAFSPDGTFVASSSQDGTIKLWDL-------RTGKCVATLTGH 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2981 TQAVTCLTASVTFSLLVSGSQDRTCILWDLDHLSRVACLPVHREGISAIAISDVSGTIVSCAGA-HLSLWNV-NGQPLAS 3058
Cdd:cd00200    177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDgTIRVWDLrTGECVQT 256

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1767181131 3059 ITtawGPEGTITCCcivegpAWDAS-HVIITGSKDGMVRIWK 3099
Cdd:cd00200    257 LS---GHTNSVTSL------AWSPDgKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
2943-3102 2.41e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 87.27  E-value: 2.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2943 SP--TMIVTSGASAVVCIWELSlvkgrprGLKLRQALYGHTQAVTcltaSVTFS----LLVSGSQDRTCILWDLDHLSRV 3016
Cdd:COG2319    255 SPdgRLLASGSADGTVRLWDLA-------TGELLRTLTGHSGGVN----SVAFSpdgkLLASGSDDGTVRLWDLATGKLL 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 3017 ACLPVHREGISAIAISDVSGTIVS-CAGAHLSLWNVNGQPLasITTAWGPEGTITCCcivegpAWDA-SHVIITGSKDGM 3094
Cdd:COG2319    324 RTLTGHTGAVRSVAFSPDGKTLASgSDDGTVRLWDLATGEL--LRTLTGHTGAVTSV------AFSPdGRTLASGSADGT 395


                   ....*...
gi 1767181131 3095 VRIWKTED 3102
Cdd:COG2319    396 VRLWDLAT 403
WD40 pfam00400
WD domain, G-beta repeat;
2972-3009 3.53e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 3.53e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1767181131 2972 KLRQALYGHTQAVTCLTASVTFSLLVSGSQDRTCILWD 3009
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 2972-3009 1.21e-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: 1.21e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1767181131  2972 KLRQALYGHTQAVTCLTASVTFSLLVSGSQDRTCILWD 3009
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 2463-2506 6.78e-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: 6.78e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1767181131 2463 YSDLRELRQARFLLQDIALEIFFQNGYSKLLVFYN-SDRSKALKS 2506
Cdd:pfam14844   53 ISDIKEVHLRRYLLRDTALEIFLIDRTSLFFNFPDtGTRRKVYRK 97
 
Name Accession Description Interval E-value
Beach pfam02138
Beige/BEACH domain;
2538-2819 8.13e-176

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 540.91  E-value: 8.13e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2538 QRWQKREISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSEMLNLTNPKTFRDLSKPMGAQTKERKLKFTQRFKDVE 2617
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2618 kiegDMTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKSTWESASkENMSDVRELTPEFFYLP 2697
Cdd:pfam02138   81 ----DDDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKELIPEFFYLP 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2698 EFLTNCNAVEFGCMQDGTTLGDVQLPPWADGDPRKFISLHRQALESDFVSSNLHHWIDLIFGYKQQGPAAVEAVNTFHPY 2777
Cdd:pfam02138  156 EFLLNSNNFDLGGRQDGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPL 235

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1767181131 2778 FYGDRIDLGSITDPLIKSTILGFISNFGQVPKQIFTKPHPSR 2819
Cdd:pfam02138  236 TYEGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 2538-2819 1.88e-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: 525.64  E-value: 1.88e-170
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131  2538 QRWQKREISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSEMLNLTNPKTFRDLSKPMGAQTKERKLKFTQRFKDVE 2617
Cdd:smart01026    2 QKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEELE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131  2618 KIEgdmTVQCHYYTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKSTWESASKENMSDVRELTPEFFYLP 2697
Cdd:smart01026   82 DPD---IPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVKELIPEFFYLP 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131  2698 EFLTNCNAVEFGCMQDGTTLGDVQLPPWADGDPRKFISLHRQALESDFVSSNLHHWIDLIFGYKQQGPAAVEAVNTFHPY 2777
Cdd:smart01026  159 EFLVNINGFDFGTRQDGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFHPL 238

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|..
gi 1767181131  2778 FYGDRIDLGSITDPLIKSTILGFISNFGQVPKQIFTKPHPSR 2819
Cdd:smart01026  239 TYEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 2538-2819 4.24e-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: 449.77  E-value: 4.24e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2538 QRWQKREISNFEYLMYLNTLAGRTYNDYMQYPVFPWVLADYTSEMLNLTNPKTFRDLSKPMGAQTKERKlkftQRFKDVE 2617
Cdd:cd06071      2 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERL----QLLKERY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2618 KIEGDMTVQ-CHYYTHYSSAIIVASYLVRMPPFTQAFCSLQGGSFDVADRMFHSVKSTWESASkENMSDVRELTPEFFYL 2696
Cdd:cd06071     78 ESDSDDSDPpFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSAS-ENPSDVKELIPEFYYL 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2697 PEFLTNCNAVEFGCmQDGTTLGDVQLPPWADGdPRKFISLHRQALESDFVSSNLHHWIDLIFGYKQQGPAAVEAVNTFHP 2776
Cdd:cd06071    157 PEFFLNINKFDFGK-QDGEKVNDVELPPWAKS-PEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFHP 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1767181131 2777 YFYGDRIDLGSITdpLIKSTILGFISNFGQVPKQIFTKPHPSR 2819
Cdd:cd06071    235 LTYEGSVDLDSID--VEREAIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 2386-2507 3.01e-22

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: 94.22  E-value: 3.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2386 EKVSQKVPMVIVQGHLVSEGILLFGQHHFYICENFTLSPTGDVycthhclsnisdpfIFNMCSKDRSSDHYSCQRHAYSD 2465
Cdd:cd01201      1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKI--------------VVINSQKVLSYKEHLVFKWSLSD 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1767181131 2466 LRELRQARFLLQDIALEIFFQNGYSKLLVFYNSDRSKALKSF 2507
Cdd:cd01201     67 IREVHKRRYLLRDTALEIFFTDGTNYFLNFPSKERNDVYKKL 108
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2901-3099 5.13e-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: 98.95  E-value: 5.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2901 NRTFSWGFDDFSCCLGSYGSDKILMTFENLAAWGPClCAVCPSPTMIVTSGASAVVCIWELslvkgrpRGLKLRQALYGH 2980
Cdd:cd00200    105 GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS-VAFSPDGTFVASSSQDGTIKLWDL-------RTGKCVATLTGH 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2981 TQAVTCLTASVTFSLLVSGSQDRTCILWDLDHLSRVACLPVHREGISAIAISDVSGTIVSCAGA-HLSLWNV-NGQPLAS 3058
Cdd:cd00200    177 TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDgTIRVWDLrTGECVQT 256

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1767181131 3059 ITtawGPEGTITCCcivegpAWDAS-HVIITGSKDGMVRIWK 3099
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 ...
 2938-3098 1.23e-18

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 89.32  E-value: 1.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2938 CAVCPSPTMIVTSGASAVVCIWELSlvkgrpRGLKLRQaLYGHTQAVTCLTASVTFSLLVSGSQDRTCILWDLDHLSRVA 3017
Cdd:cd00200     15 VAFSPDGKLLATGSGDGTIKVWDLE------TGELLRT-LKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVR 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 3018 CLPVHREGISAIAISDvSGTIVSCAGAHLS--LWNV-NGQPLASITtawGPEGTITCCCIVEGpawdaSHVIITGSKDGM 3094
Cdd:cd00200     88 TLTGHTSYVSSVAFSP-DGRILSSSSRDKTikVWDVeTGKCLTTLR---GHTDWVNSVAFSPD-----GTFVASSSQDGT 158


                   ....
gi 1767181131 3095 VRIW 3098
Cdd:cd00200    159 IKLW 162
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2973-3104 1.51e-18

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 88.93  E-value: 1.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2973 LRQALYGHTQAVTCLTASVTFSLLVSGSQDRTCILWDLDHLSRVACLPVHREGISAIAISDVSGTIVSCAGAH-LSLWNV 3051
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKtIRLWDL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1767181131 3052 NGQPLASITTawGPEGTITCCCIVegpawDASHVIITGSKDGMVRIWKTEDVK 3104
Cdd:cd00200     81 ETGECVRTLT--GHTSYVSSVAFS-----PDGRILSSSSRDKTIKVWDVETGK 126
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2907-3101 2.10e-18

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 88.55  E-value: 2.10e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2907 GFDDFSCCLGSYGSDKILMTFENLAAWGPClCAVCPSPTMIVTSGASAVVCIWELslvkgrpRGLKLRQALYGHTQAVTC 2986
Cdd:cd00200     69 GSSDKTIRLWDLETGECVRTLTGHTSYVSS-VAFSPDGRILSSSSRDKTIKVWDV-------ETGKCLTTLRGHTDWVNS 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2987 LTASVTFSLLVSGSQDRTCILWDLDHLSRVACLPVHREGISAIAISDVSGTIVSCAG-AHLSLWNVNGQplASITTAWGP 3065
Cdd:cd00200    141 VAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSdGTIKLWDLSTG--KCLGTLRGH 218

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1767181131 3066 EGTITCCcivegpAWDASHVIIT-GSKDGMVRIWKTE 3101
Cdd:cd00200    219 ENGVNSV------AFSPDGYLLAsGSEDGTIRVWDLR 249
WD40 COG2319
WD40 repeat [General function prediction only];
2943-3102 2.41e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 87.27  E-value: 2.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2943 SP--TMIVTSGASAVVCIWELSlvkgrprGLKLRQALYGHTQAVTcltaSVTFS----LLVSGSQDRTCILWDLDHLSRV 3016
Cdd:COG2319    255 SPdgRLLASGSADGTVRLWDLA-------TGELLRTLTGHSGGVN----SVAFSpdgkLLASGSDDGTVRLWDLATGKLL 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 3017 ACLPVHREGISAIAISDVSGTIVS-CAGAHLSLWNVNGQPLasITTAWGPEGTITCCcivegpAWDA-SHVIITGSKDGM 3094
Cdd:COG2319    324 RTLTGHTGAVRSVAFSPDGKTLASgSDDGTVRLWDLATGEL--LRTLTGHTGAVTSV------AFSPdGRTLASGSADGT 395


                   ....*...
gi 1767181131 3095 VRIWKTED 3102
Cdd:COG2319    396 VRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
2939-3183 4.44e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 86.50  E-value: 4.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2939 AVCPSPTMIVTSGASAVVCIWELslvkgrpRGLKLRQALYGHTQAVTcltaSVTFS----LLVSGSQDRTCILWDLDHLS 3014
Cdd:COG2319    211 AFSPDGKLLASGSADGTVRLWDL-------ATGKLLRTLTGHSGSVR----SVAFSpdgrLLASGSADGTVRLWDLATGE 279

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 3015 RVACLPVHREGISAIAISDVSGTIVS-CAGAHLSLWNVN-GQPLASITtawGPEGTITCCcivegpAWDA-SHVIITGSK 3091
Cdd:COG2319    280 LLRTLTGHSGGVNSVAFSPDGKLLASgSDDGTVRLWDLAtGKLLRTLT---GHTGAVRSV------AFSPdGKTLASGSD 350

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 3092 DGMVRIWKTEDVKmpvprqavmeepstEPLSPRGHkwaknlalsreldvsvalsgkpskaSPAVTALAITRNQSKLLVGD 3171
Cdd:COG2319    351 DGTVRLWDLATGE--------------LLRTLTGH-------------------------TGAVTSVAFSPDGRTLASGS 391

                          250
                   ....*....|..
gi 1767181131 3172 EKGRIFCWSADG 3183
Cdd:COG2319    392 ADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
2939-3183 1.08e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 85.35  E-value: 1.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2939 AVCPSP--TMIVTSGASAVVCIWELslvkgrpRGLKLRQALYGHTQAVTcltaSVTFS----LLVSGSQDRTCILWDLDH 3012
Cdd:COG2319    125 SVAFSPdgKTLASGSADGTVRLWDL-------ATGKLLRTLTGHSGAVT----SVAFSpdgkLLASGSDDGTVRLWDLAT 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 3013 LSRVACLPVHREGISAIAISDVSGTIVSCAGAH-LSLWNVN-GQPLASITtawGPEGTITCCcivegpAWDA-SHVIITG 3089
Cdd:COG2319    194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGtVRLWDLAtGKLLRTLT---GHSGSVRSV------AFSPdGRLLASG 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 3090 SKDGMVRIWKTEDvkmpvprqavmeepSTEPLSPRGHK-WAKNLALSRE--------LDVSVAL----SGKPSKA----S 3152
Cdd:COG2319    265 SADGTVRLWDLAT--------------GELLRTLTGHSgGVNSVAFSPDgkllasgsDDGTVRLwdlaTGKLLRTltghT 330

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1767181131 3153 PAVTALAITRNQSKLLVGDEKGRIFCWSADG 3183
Cdd:COG2319    331 GAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361
WD40 COG2319
WD40 repeat [General function prediction only];
2948-3183 7.33e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.49  E-value: 7.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2948 VTSGASAVVCIWELSLVKGRPRGLKLRQALYGHTQAVTCLTASVTFSLLVSGSQDRTCILWDLDHLSRVACLPVHREGIS 3027
Cdd:COG2319     45 SPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVR 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 3028 AIAISDVSGTIVSCAGAH-LSLWNV-NGQPLASITtawGPEGTITCCcivegpAWDA-SHVIITGSKDGMVRIWKTEDVK 3104
Cdd:COG2319    125 SVAFSPDGKTLASGSADGtVRLWDLaTGKLLRTLT---GHSGAVTSV------AFSPdGKLLASGSDDGTVRLWDLATGK 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 3105 mpvprqavmeepstEPLSPRGHK-WAKNLALSRE--------LDVSVAL----SGKPSKA----SPAVTALAITRNQSKL 3167
Cdd:COG2319    196 --------------LLRTLTGHTgAVRSVAFSPDgkllasgsADGTVRLwdlaTGKLLRTltghSGSVRSVAFSPDGRLL 261

                          250
                   ....*....|....*.
gi 1767181131 3168 LVGDEKGRIFCWSADG 3183
Cdd:COG2319    262 ASGSADGTVRLWDLAT 277
WD40 pfam00400
WD domain, G-beta repeat;
2972-3009 3.53e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 3.53e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1767181131 2972 KLRQALYGHTQAVTCLTASVTFSLLVSGSQDRTCILWD 3009
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 2972-3009 1.21e-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: 1.21e-05
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1767181131  2972 KLRQALYGHTQAVTCLTASVTFSLLVSGSQDRTCILWD 3009
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 2463-2506 6.78e-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: 6.78e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1767181131 2463 YSDLRELRQARFLLQDIALEIFFQNGYSKLLVFYN-SDRSKALKS 2506
Cdd:pfam14844   53 ISDIKEVHLRRYLLRDTALEIFLIDRTSLFFNFPDtGTRRKVYRK 97
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 2939-3058 9.65e-05

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


Pssm-ID: 466575 [Multi-domain]  Cd Length: 350  Bit Score: 47.37  E-value: 9.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 2939 AVCPSPTMIVTSGASAVVCIWELSLVKGRPRGLKLRQA----------------LYGHTQAVTCLTASVTFSLLVSGSQD 3002
Cdd:pfam20426  131 AVTSDGSILATGSYDTTVMVWEVLRGRSSEKRSRNTQTefprkdhviaetpfhiLCGHDDIITCLYVSVELDIVISGSKD 210

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767181131 3003 RTCILWDLDHLSRVACL--PvHREGISAIAISDvSGTIVSCAGAHLSL--WNVNGQPLAS 3058
Cdd:pfam20426  211 GTCIFHTLREGRYVRSIrhP-SGCPLSKLVASR-HGRIVLYADDDLSLhlYSINGKHIAS 268
 
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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