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Conserved domains on  [gi|1580781|gb|AAB09603|]
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beige-like protein, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Beach pfam02138
Beige/BEACH domain;
1439-1715 0e+00

Beige/BEACH domain;


:

Pssm-ID: 460459  Cd Length: 277  Bit Score: 560.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1439 QRWQHREISNFEYLMFLNTIAGRSYNDLNQYPVFPWVITNYESEELDLTLPTNFRDLSKPIGALNPKRAAFFAERYESWE 1518
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1519 DDQvPKFHYGTHYSTASFVLAWLLRIEPFTTYFLNLQGGKFDHADRTFSSISRAWRNSQRDTSDIKELIPEFYYLPEMFV 1598
Cdd:pfam02138   81 DDD-PPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSASNSTSDVKELIPEFFYLPEFLL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1599 NFNNYNLGVMDDGTVVSDVELPPWAKTS-EEFVHINRLALESEFVSCQLHQWIDLIFGYKQQGPEAVRALNVFYYLTYEG 1677
Cdd:pfam02138  160 NSNNFDLGGRQDGEKVDDVELPPWAKKSpEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPLTYEG 239

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1580781    1678 AVNLNSITDPVLREAVEAQIRSFGQTPSQLLIEPHPPR 1715
Cdd:pfam02138  240 SVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
DUF1088 pfam06469
Neurobeachin-like, DUF1088; This domain is found in the neurobeachins (NBEAs) and BEACH domain ...
 1106-1284 3.31e-97

Neurobeachin-like, DUF1088; This domain is found in the neurobeachins (NBEAs) and BEACH domain containing proteins (BDCPs). NBEAS are localized near Golgi apparatus and is involved in vesicular trafficking, intracellular transport, membrane dynamics, endosomal recycling, and receptor signalling. BDCPs are associated with lysosome size, apoptosis, autophagy, granule size, or synapse formation. Mutations in this domain have been related to autosomal recessively inherited lipopolysaccharide-responsive beige-like anchor (LRBA) protein deficiency, responsible for common variable immunodeficiency (CVID) and autoimmune lymphoproliferative syndrome (ALPS). NBEAs deficiency may induce spine loss with defects in synaptic efficacy and plasticity, being associated with autism spectrum disorder (ASD) and ASD-related syndromes.


:

Pssm-ID: 461925  Cd Length: 168  Bit Score: 310.29  E-value: 3.31e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1106 EGRLLSQTMKDHLVRVANEAEFILSRQRAEDIHRHAEFESLCAQYSADKREDEKMCDHLIRAAKYRDHVTATQLIQKIIN 1185
Cdd:pfam06469    1 EGRLLSHAMKDHVVRVANEAEFILNRQRAEDVHKHAEFESECAQYLADRREEEKMCDHLITAAKRRDHVTATQLLQKIVN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1186 ILTDKHGAWGNSAVSRPLEFWRLDYWEDDLRRRRRFVRNPLGSTHPEATLKTAVEHvcifklrenskATDEDILAKGKQS 1265
Cdd:pfam06469   81 ILTNKHGAWGYPNQSRLSEFWRLDYWEDDLRRRRRFVRNPYGSTHPEATLKSAQEH-----------ALPEDRIVKSKLV 149

                          170
                   ....*....|....*....
gi 1580781    1266 IRSQALGNQNSENEILLEG 1284
Cdd:pfam06469  150 FRSQRLASQNSETELVLDG 168
DUF4704 super family cl24375
Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in ...
 5-147 7.62e-56

Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in eukaryotes on neurobeachin and BEACH domain-containing proteins (BDCPs). Mutations in this proteins are associated with Lipopolysaccharide-responsive and beige-like anchor (LRBA) deficiency. According to structure prediction is adopts an alpha-helical solenoid structure.


The actual alignment was detected with superfamily member pfam15787:

Pssm-ID: 464870  Cd Length: 486  Bit Score: 202.90  E-value: 7.62e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781       5 ITMTTYNVLFEILIEQIGTQVIHKQHPDPDSSVKIQNPQILKVIATLLRNSPQCpESMEVRRAFLSDMIKLFNNSRENRR 84
Cdd:pfam15787  344 LTDPTYNVLFEILLGGASPQQVYEKHSEPEKHSRFENPQILKVIFRLLRQSKDS-ESMMLRKLFLSDLLNLLNSNRANRR 422

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1580781      85 SLLQCSVWQEWMLSLCYFNPKNSDE-QKITEMVYAIFRILLYHAVKYEWGGWRVWVDTLSITHS 147
Cdd:pfam15787  423 TLLQMSVWQEWLFSSAYLAPIKNYEqQNETELVYSLFRILLHHALKNEKGGWRVWVDTLAILHS 486
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 1310-1407 4.84e-34

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: 126.61  E-value: 4.84e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1310 AQLVAPSVVVKGTLSVTSSELYFEVDEED-PNFKKIDPKILAYTEGLHGKWLFTEIRSIFSRRYLLQNTALEIFMANRVA 1388
Cdd:pfam14844    1 CELVTPMGVVRGKLSITTDHIYFTADDEDeALDSVQESESLGYDKPKHKRWPISDIKEVHLRRYLLRDTALEIFLIDRTS 80

                           90
                   ....*....|....*....
gi 1580781    1389 VMFNFPDPATVKKVVNFLP 1407
Cdd:pfam14844   81 LFFNFPDTGTRRKVYRKLV 99
NBCH_WD40 super family cl48581
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 1810-1896 3.37e-10

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


The actual alignment was detected with superfamily member pfam20426:

Pssm-ID: 466575 [Multi-domain]  Cd Length: 350  Bit Score: 63.94  E-value: 3.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1810 RQITDLLDQSIQVHSQCFV---ITSDNrYILVCGFWDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSESyigGNcYILSG 1886
Cdd:pfam20426   68 RKIGSPLAENVELGAQCFAtlqTPSEN-FLISCGNWENSFQVISLNDGRMVQSIRQHKDVVSCVAVTSD---GS-ILATG 142

                           90
                   ....*....|
gi 1580781    1887 SRDATLLLWY 1896
Cdd:pfam20426  143 SYDTTVMVWE 152
motB super family cl32828
flagellar motor protein MotB; Reviewed
 858-1021 1.48e-03

flagellar motor protein MotB; Reviewed


The actual alignment was detected with superfamily member PRK12799:

Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 43.17  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    858 AGPDAISEVLSTLSLevNKSPETKNDRGNdLDTKAtpsVSVSKNVNVKDI----LRSLVNIPADGVTVDPALLPPACLGA 933
Cdd:PRK12799  250 ASDDPVNRRISILVL--NKQSQHDIEHEN-LDNRA---LDIEKATGLKQIdthgTVPVAAVTPSSAVTQSSAITPSSAAI 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    934 LGDLSVEQPVQFRSFD--RSVIVAAKKSAVSPSTFNTSI--------PTNAVSVVSSVDSAQASDMGGESPGSRSSNAKL 1003
Cdd:PRK12799  324 PSPAVIPSSVTTQSATttQASAVALSSAGVLPSDVTLPGtvalpaaePVNMQPQPMSTTETQQSSTGNITSTANGPTTSL 403

                         170
                  ....*....|....*...
gi 1580781   1004 PSVPTvdsvSQDPVSNMS 1021
Cdd:PRK12799  404 PAAPA----SNIPVSPTS 417
 
Name Accession Description Interval E-value
Beach pfam02138
Beige/BEACH domain;
1439-1715 0e+00

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 560.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1439 QRWQHREISNFEYLMFLNTIAGRSYNDLNQYPVFPWVITNYESEELDLTLPTNFRDLSKPIGALNPKRAAFFAERYESWE 1518
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1519 DDQvPKFHYGTHYSTASFVLAWLLRIEPFTTYFLNLQGGKFDHADRTFSSISRAWRNSQRDTSDIKELIPEFYYLPEMFV 1598
Cdd:pfam02138   81 DDD-PPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSASNSTSDVKELIPEFFYLPEFLL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1599 NFNNYNLGVMDDGTVVSDVELPPWAKTS-EEFVHINRLALESEFVSCQLHQWIDLIFGYKQQGPEAVRALNVFYYLTYEG 1677
Cdd:pfam02138  160 NSNNFDLGGRQDGEKVDDVELPPWAKKSpEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPLTYEG 239

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1580781    1678 AVNLNSITDPVLREAVEAQIRSFGQTPSQLLIEPHPPR 1715
Cdd:pfam02138  240 SVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 1438-1715 0e+00

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: 559.92  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781     1438 TQRWQHREISNFEYLMFLNTIAGRSYNDLNQYPVFPWVITNYESEELDLTLPTNFRDLSKPIGALNPKRAAFFAERYESW 1517
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781     1518 EDDQVPKFHYGTHYSTASFVLAWLLRIEPFTTYFLNLQGGKFDHADRTFSSISRAWRN-SQRDTSDIKELIPEFYYLPEM 1596
Cdd:smart01026   81 EDPDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSaSLESMTDVKELIPEFFYLPEF 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781     1597 FVNFNNYNLGVMDDGTVVSDVELPPWAKTS-EEFVHINRLALESEFVSCQLHQWIDLIFGYKQQGPEAVRALNVFYYLTY 1675
Cdd:smart01026  161 LVNINGFDFGTRQDGEDVDDVELPPWAKGSpEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFHPLTY 240

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|
gi 1580781     1676 EGAVNLNSITDPVLREAVEAQIRSFGQTPSQLLIEPHPPR 1715
Cdd:smart01026  241 EGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 1438-1715 1.07e-162

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: 497.92  E-value: 1.07e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1438 TQRWQHREISNFEYLMFLNTIAGRSYNDLNQYPVFPWVITNYESEELDLTLPTNFRDLSKPIGALNPKRAAFFAERYESW 1517
Cdd:cd06071    1 TKKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERYESD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1518 EDDQVPKFHYGTHYSTASFVLAWLLRIEPFTTYFLNLQGGKFDHADRTFSSISRAWRNSQRDTSDIKELIPEFYYLPEMF 1597
Cdd:cd06071   81 SDDSDPPFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSASENPSDVKELIPEFYYLPEFF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1598 VNFNNYNLGVmDDGTVVSDVELPPWAKTSEEFVHINRLALESEFVSCQLHQWIDLIFGYKQQGPEAVRALNVFYYLTYEG 1677
Cdd:cd06071  161 LNINKFDFGK-QDGEKVNDVELPPWAKSPEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFHPLTYEG 239

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 1580781  1678 AVNLNSITdpVLREAVEAQIRSFGQTPSQLLIEPHPPR 1715
Cdd:cd06071  240 SVDLDSID--VEREAIEAQINNFGQTPVQLFTKPHPKR 275
DUF1088 pfam06469
Neurobeachin-like, DUF1088; This domain is found in the neurobeachins (NBEAs) and BEACH domain ...
 1106-1284 3.31e-97

Neurobeachin-like, DUF1088; This domain is found in the neurobeachins (NBEAs) and BEACH domain containing proteins (BDCPs). NBEAS are localized near Golgi apparatus and is involved in vesicular trafficking, intracellular transport, membrane dynamics, endosomal recycling, and receptor signalling. BDCPs are associated with lysosome size, apoptosis, autophagy, granule size, or synapse formation. Mutations in this domain have been related to autosomal recessively inherited lipopolysaccharide-responsive beige-like anchor (LRBA) protein deficiency, responsible for common variable immunodeficiency (CVID) and autoimmune lymphoproliferative syndrome (ALPS). NBEAs deficiency may induce spine loss with defects in synaptic efficacy and plasticity, being associated with autism spectrum disorder (ASD) and ASD-related syndromes.


Pssm-ID: 461925  Cd Length: 168  Bit Score: 310.29  E-value: 3.31e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1106 EGRLLSQTMKDHLVRVANEAEFILSRQRAEDIHRHAEFESLCAQYSADKREDEKMCDHLIRAAKYRDHVTATQLIQKIIN 1185
Cdd:pfam06469    1 EGRLLSHAMKDHVVRVANEAEFILNRQRAEDVHKHAEFESECAQYLADRREEEKMCDHLITAAKRRDHVTATQLLQKIVN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1186 ILTDKHGAWGNSAVSRPLEFWRLDYWEDDLRRRRRFVRNPLGSTHPEATLKTAVEHvcifklrenskATDEDILAKGKQS 1265
Cdd:pfam06469   81 ILTNKHGAWGYPNQSRLSEFWRLDYWEDDLRRRRRFVRNPYGSTHPEATLKSAQEH-----------ALPEDRIVKSKLV 149

                          170
                   ....*....|....*....
gi 1580781    1266 IRSQALGNQNSENEILLEG 1284
Cdd:pfam06469  150 FRSQRLASQNSETELVLDG 168
DUF4704 pfam15787
Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in ...
 5-147 7.62e-56

Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in eukaryotes on neurobeachin and BEACH domain-containing proteins (BDCPs). Mutations in this proteins are associated with Lipopolysaccharide-responsive and beige-like anchor (LRBA) deficiency. According to structure prediction is adopts an alpha-helical solenoid structure.


Pssm-ID: 464870  Cd Length: 486  Bit Score: 202.90  E-value: 7.62e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781       5 ITMTTYNVLFEILIEQIGTQVIHKQHPDPDSSVKIQNPQILKVIATLLRNSPQCpESMEVRRAFLSDMIKLFNNSRENRR 84
Cdd:pfam15787  344 LTDPTYNVLFEILLGGASPQQVYEKHSEPEKHSRFENPQILKVIFRLLRQSKDS-ESMMLRKLFLSDLLNLLNSNRANRR 422

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1580781      85 SLLQCSVWQEWMLSLCYFNPKNSDE-QKITEMVYAIFRILLYHAVKYEWGGWRVWVDTLSITHS 147
Cdd:pfam15787  423 TLLQMSVWQEWLFSSAYLAPIKNYEqQNETELVYSLFRILLHHALKNEKGGWRVWVDTLAILHS 486
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 1310-1407 4.84e-34

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: 126.61  E-value: 4.84e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1310 AQLVAPSVVVKGTLSVTSSELYFEVDEED-PNFKKIDPKILAYTEGLHGKWLFTEIRSIFSRRYLLQNTALEIFMANRVA 1388
Cdd:pfam14844    1 CELVTPMGVVRGKLSITTDHIYFTADDEDeALDSVQESESLGYDKPKHKRWPISDIKEVHLRRYLLRDTALEIFLIDRTS 80

                           90
                   ....*....|....*....
gi 1580781    1389 VMFNFPDPATVKKVVNFLP 1407
Cdd:pfam14844   81 LFFNFPDTGTRRKVYRKLV 99
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 1303-1406 1.07e-33

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: 126.20  E-value: 1.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1303 PVSLSTPAQLVAPSVVVKGTLSVTSSELYFEVDEEDPNFKKID----PKILAYTEGLHGKWLFTEIRSIFSRRYLLQNTA 1378
Cdd:cd01201    2 KILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVvinsQKVLSYKEHLVFKWSLSDIREVHKRRYLLRDTA 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 1580781  1379 LEIFMANRVAVMFNFPDPA---TVKKVVNFL 1406
Cdd:cd01201   82 LEIFFTDGTNYFLNFPSKErndVYKKLLSLL 112
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 1810-1896 3.37e-10

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: 63.94  E-value: 3.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1810 RQITDLLDQSIQVHSQCFV---ITSDNrYILVCGFWDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSESyigGNcYILSG 1886
Cdd:pfam20426   68 RKIGSPLAENVELGAQCFAtlqTPSEN-FLISCGNWENSFQVISLNDGRMVQSIRQHKDVVSCVAVTSD---GS-ILATG 142

                           90
                   ....*....|
gi 1580781    1887 SRDATLLLWY 1896
Cdd:pfam20426  143 SYDTTVMVWE 152
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1831-1895 7.03e-08

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 56.19  E-value: 7.03e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1580781  1831 SDNRYILVCGFWDKSFRVYSTDTGRLIQVVFGHWDVVTCLArsesYIGGNCYILSGSRDATLLLW 1895
Cdd:cd00200  102 SPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVA----FSPDGTFVASSSQDGTIKLW 162
WD40 COG2319
WD40 repeat [General function prediction only];
1777-1895 3.16e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.84  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1777 HNLPAHQGAVQDqpyqlpVEIDP---LIAS------------NTGmhrRQITDLLDQSIQVHSqcFVITSDNRYILVCGf 1841
Cdd:COG2319  198 RTLTGHTGAVRS------VAFSPdgkLLASgsadgtvrlwdlATG---KLLRTLTGHSGSVRS--VAFSPDGRLLASGS- 265

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1580781  1842 WDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSESyigGNcYILSGSRDATLLLW 1895
Cdd:COG2319  266 ADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPD---GK-LLASGSDDGTVRLW 315
motB PRK12799
flagellar motor protein MotB; Reviewed
 858-1021 1.48e-03

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 43.17  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    858 AGPDAISEVLSTLSLevNKSPETKNDRGNdLDTKAtpsVSVSKNVNVKDI----LRSLVNIPADGVTVDPALLPPACLGA 933
Cdd:PRK12799  250 ASDDPVNRRISILVL--NKQSQHDIEHEN-LDNRA---LDIEKATGLKQIdthgTVPVAAVTPSSAVTQSSAITPSSAAI 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    934 LGDLSVEQPVQFRSFD--RSVIVAAKKSAVSPSTFNTSI--------PTNAVSVVSSVDSAQASDMGGESPGSRSSNAKL 1003
Cdd:PRK12799  324 PSPAVIPSSVTTQSATttQASAVALSSAGVLPSDVTLPGtvalpaaePVNMQPQPMSTTETQQSSTGNITSTANGPTTSL 403

                         170
                  ....*....|....*...
gi 1580781   1004 PSVPTvdsvSQDPVSNMS 1021
Cdd:PRK12799  404 PAAPA----SNIPVSPTS 417
 
Name Accession Description Interval E-value
Beach pfam02138
Beige/BEACH domain;
1439-1715 0e+00

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 560.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1439 QRWQHREISNFEYLMFLNTIAGRSYNDLNQYPVFPWVITNYESEELDLTLPTNFRDLSKPIGALNPKRAAFFAERYESWE 1518
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEELE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1519 DDQvPKFHYGTHYSTASFVLAWLLRIEPFTTYFLNLQGGKFDHADRTFSSISRAWRNSQRDTSDIKELIPEFYYLPEMFV 1598
Cdd:pfam02138   81 DDD-PPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSASNSTSDVKELIPEFFYLPEFLL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1599 NFNNYNLGVMDDGTVVSDVELPPWAKTS-EEFVHINRLALESEFVSCQLHQWIDLIFGYKQQGPEAVRALNVFYYLTYEG 1677
Cdd:pfam02138  160 NSNNFDLGGRQDGEKVDDVELPPWAKKSpEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHPLTYEG 239

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1580781    1678 AVNLNSITDPVLREAVEAQIRSFGQTPSQLLIEPHPPR 1715
Cdd:pfam02138  240 SVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 1438-1715 0e+00

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: 559.92  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781     1438 TQRWQHREISNFEYLMFLNTIAGRSYNDLNQYPVFPWVITNYESEELDLTLPTNFRDLSKPIGALNPKRAAFFAERYESW 1517
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781     1518 EDDQVPKFHYGTHYSTASFVLAWLLRIEPFTTYFLNLQGGKFDHADRTFSSISRAWRN-SQRDTSDIKELIPEFYYLPEM 1596
Cdd:smart01026   81 EDPDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSaSLESMTDVKELIPEFFYLPEF 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781     1597 FVNFNNYNLGVMDDGTVVSDVELPPWAKTS-EEFVHINRLALESEFVSCQLHQWIDLIFGYKQQGPEAVRALNVFYYLTY 1675
Cdd:smart01026  161 LVNINGFDFGTRQDGEDVDDVELPPWAKGSpEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFHPLTY 240

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|
gi 1580781     1676 EGAVNLNSITDPVLREAVEAQIRSFGQTPSQLLIEPHPPR 1715
Cdd:smart01026  241 EGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 1438-1715 1.07e-162

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: 497.92  E-value: 1.07e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1438 TQRWQHREISNFEYLMFLNTIAGRSYNDLNQYPVFPWVITNYESEELDLTLPTNFRDLSKPIGALNPKRAAFFAERYESW 1517
Cdd:cd06071    1 TKKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERYESD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1518 EDDQVPKFHYGTHYSTASFVLAWLLRIEPFTTYFLNLQGGKFDHADRTFSSISRAWRNSQRDTSDIKELIPEFYYLPEMF 1597
Cdd:cd06071   81 SDDSDPPFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSASENPSDVKELIPEFYYLPEFF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1598 VNFNNYNLGVmDDGTVVSDVELPPWAKTSEEFVHINRLALESEFVSCQLHQWIDLIFGYKQQGPEAVRALNVFYYLTYEG 1677
Cdd:cd06071  161 LNINKFDFGK-QDGEKVNDVELPPWAKSPEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFHPLTYEG 239

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 1580781  1678 AVNLNSITdpVLREAVEAQIRSFGQTPSQLLIEPHPPR 1715
Cdd:cd06071  240 SVDLDSID--VEREAIEAQINNFGQTPVQLFTKPHPKR 275
DUF1088 pfam06469
Neurobeachin-like, DUF1088; This domain is found in the neurobeachins (NBEAs) and BEACH domain ...
 1106-1284 3.31e-97

Neurobeachin-like, DUF1088; This domain is found in the neurobeachins (NBEAs) and BEACH domain containing proteins (BDCPs). NBEAS are localized near Golgi apparatus and is involved in vesicular trafficking, intracellular transport, membrane dynamics, endosomal recycling, and receptor signalling. BDCPs are associated with lysosome size, apoptosis, autophagy, granule size, or synapse formation. Mutations in this domain have been related to autosomal recessively inherited lipopolysaccharide-responsive beige-like anchor (LRBA) protein deficiency, responsible for common variable immunodeficiency (CVID) and autoimmune lymphoproliferative syndrome (ALPS). NBEAs deficiency may induce spine loss with defects in synaptic efficacy and plasticity, being associated with autism spectrum disorder (ASD) and ASD-related syndromes.


Pssm-ID: 461925  Cd Length: 168  Bit Score: 310.29  E-value: 3.31e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1106 EGRLLSQTMKDHLVRVANEAEFILSRQRAEDIHRHAEFESLCAQYSADKREDEKMCDHLIRAAKYRDHVTATQLIQKIIN 1185
Cdd:pfam06469    1 EGRLLSHAMKDHVVRVANEAEFILNRQRAEDVHKHAEFESECAQYLADRREEEKMCDHLITAAKRRDHVTATQLLQKIVN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1186 ILTDKHGAWGNSAVSRPLEFWRLDYWEDDLRRRRRFVRNPLGSTHPEATLKTAVEHvcifklrenskATDEDILAKGKQS 1265
Cdd:pfam06469   81 ILTNKHGAWGYPNQSRLSEFWRLDYWEDDLRRRRRFVRNPYGSTHPEATLKSAQEH-----------ALPEDRIVKSKLV 149

                          170
                   ....*....|....*....
gi 1580781    1266 IRSQALGNQNSENEILLEG 1284
Cdd:pfam06469  150 FRSQRLASQNSETELVLDG 168
DUF4704 pfam15787
Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in ...
 5-147 7.62e-56

Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in eukaryotes on neurobeachin and BEACH domain-containing proteins (BDCPs). Mutations in this proteins are associated with Lipopolysaccharide-responsive and beige-like anchor (LRBA) deficiency. According to structure prediction is adopts an alpha-helical solenoid structure.


Pssm-ID: 464870  Cd Length: 486  Bit Score: 202.90  E-value: 7.62e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781       5 ITMTTYNVLFEILIEQIGTQVIHKQHPDPDSSVKIQNPQILKVIATLLRNSPQCpESMEVRRAFLSDMIKLFNNSRENRR 84
Cdd:pfam15787  344 LTDPTYNVLFEILLGGASPQQVYEKHSEPEKHSRFENPQILKVIFRLLRQSKDS-ESMMLRKLFLSDLLNLLNSNRANRR 422

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1580781      85 SLLQCSVWQEWMLSLCYFNPKNSDE-QKITEMVYAIFRILLYHAVKYEWGGWRVWVDTLSITHS 147
Cdd:pfam15787  423 TLLQMSVWQEWLFSSAYLAPIKNYEqQNETELVYSLFRILLHHALKNEKGGWRVWVDTLAILHS 486
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 1310-1407 4.84e-34

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: 126.61  E-value: 4.84e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1310 AQLVAPSVVVKGTLSVTSSELYFEVDEED-PNFKKIDPKILAYTEGLHGKWLFTEIRSIFSRRYLLQNTALEIFMANRVA 1388
Cdd:pfam14844    1 CELVTPMGVVRGKLSITTDHIYFTADDEDeALDSVQESESLGYDKPKHKRWPISDIKEVHLRRYLLRDTALEIFLIDRTS 80

                           90
                   ....*....|....*....
gi 1580781    1389 VMFNFPDPATVKKVVNFLP 1407
Cdd:pfam14844   81 LFFNFPDTGTRRKVYRKLV 99
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 1303-1406 1.07e-33

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: 126.20  E-value: 1.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1303 PVSLSTPAQLVAPSVVVKGTLSVTSSELYFEVDEEDPNFKKID----PKILAYTEGLHGKWLFTEIRSIFSRRYLLQNTA 1378
Cdd:cd01201    2 KILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVvinsQKVLSYKEHLVFKWSLSDIREVHKRRYLLRDTA 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 1580781  1379 LEIFMANRVAVMFNFPDPA---TVKKVVNFL 1406
Cdd:cd01201   82 LEIFFTDGTNYFLNFPSKErndVYKKLLSLL 112
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 1810-1896 3.37e-10

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: 63.94  E-value: 3.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    1810 RQITDLLDQSIQVHSQCFV---ITSDNrYILVCGFWDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSESyigGNcYILSG 1886
Cdd:pfam20426   68 RKIGSPLAENVELGAQCFAtlqTPSEN-FLISCGNWENSFQVISLNDGRMVQSIRQHKDVVSCVAVTSD---GS-ILATG 142

                           90
                   ....*....|
gi 1580781    1887 SRDATLLLWY 1896
Cdd:pfam20426  143 SYDTTVMVWE 152
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1831-1895 7.03e-08

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 56.19  E-value: 7.03e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1580781  1831 SDNRYILVCGFWDKSFRVYSTDTGRLIQVVFGHWDVVTCLArsesYIGGNCYILSGSRDATLLLW 1895
Cdd:cd00200  102 SPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVA----FSPDGTFVASSSQDGTIKLW 162
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1818-1895 1.10e-07

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 55.42  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1818 QSIQVHSQ--CFVITSDNRYILVCGFWDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSESYiggnCYILSGSRDATLLLW 1895
Cdd:cd00200  213 GTLRGHENgvNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDG----KRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
1777-1895 3.16e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.84  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1777 HNLPAHQGAVQDqpyqlpVEIDP---LIAS------------NTGmhrRQITDLLDQSIQVHSqcFVITSDNRYILVCGf 1841
Cdd:COG2319  198 RTLTGHTGAVRS------VAFSPdgkLLASgsadgtvrlwdlATG---KLLRTLTGHSGSVRS--VAFSPDGRLLASGS- 265

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 1580781  1842 WDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSESyigGNcYILSGSRDATLLLW 1895
Cdd:COG2319  266 ADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPD---GK-LLASGSDDGTVRLW 315
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1813-1895 7.53e-06

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: 50.03  E-value: 7.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1813 TDLLDQSIQVHS---QCFVITSDNRYILVCGfWDKSFRVYSTDTGRLIQVVFGHWDVVTCLArsesYIGGNCYILSGSRD 1889
Cdd:cd00200   40 TGELLRTLKGHTgpvRDVAASADGTYLASGS-SDKTIRLWDLETGECVRTLTGHTSYVSSVA----FSPDGRILSSSSRD 114


                 ....*.
gi 1580781  1890 ATLLLW 1895
Cdd:cd00200  115 KTIKVW 120
WD40 COG2319
WD40 repeat [General function prediction only];
1809-1907 1.05e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 49.91  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1809 RRQITDLLDQSIQVHSqcFVITSDNRYILVCGfWDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSESyigGNcYILSGSR 1888
Cdd:COG2319  278 GELLRTLTGHSGGVNS--VAFSPDGKLLASGS-DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPD---GK-TLASGSD 350

                         90
                 ....*....|....*....
gi 1580781  1889 DATLLLWYWNGNAVGLEIT 1907
Cdd:COG2319  351 DGTVRLWDLATGELLRTLT 369
WD40 COG2319
WD40 repeat [General function prediction only];
1809-1895 2.04e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 49.14  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1809 RRQITDLLDQSIQVHSqcFVITSDNRYILVCGfWDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSESyiggNCYILSGSR 1888
Cdd:COG2319  320 GKLLRTLTGHTGAVRS--VAFSPDGKTLASGS-DDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPD----GRTLASGSA 392


                 ....*..
gi 1580781  1889 DATLLLW 1895
Cdd:COG2319  393 DGTVRLW 399
WD40 COG2319
WD40 repeat [General function prediction only];
1810-1895 2.47e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 48.75  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1810 RQITDLLDQSIQVHSqcFVITSDNRYiLVCGFWDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSESyigGNcYILSGSRD 1889
Cdd:COG2319  153 KLLRTLTGHSGAVTS--VAFSPDGKL-LASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPD---GK-LLASGSAD 225


                 ....*.
gi 1580781  1890 ATLLLW 1895
Cdd:COG2319  226 GTVRLW 231
WD40 COG2319
WD40 repeat [General function prediction only];
1828-1895 3.77e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 48.37  E-value: 3.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1580781  1828 VITSDNRYILVCGfWDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSesyiGGNCYILSGSRDATLLLW 1895
Cdd:COG2319  127 AFSPDGKTLASGS-ADGTVRLWDLATGKLLRTLTGHSGAVTSVAFS----PDGKLLASGSDDGTVRLW 189
WD40 COG2319
WD40 repeat [General function prediction only];
1742-1895 1.90e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.06  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1742 SNSPVTHVAANTQPGLATPAVITVTANRLFAVNKWHNLPAHQGAVQDQPYQLPVEIDPLIASNTGMHRRQITDLLDQSIQ 1821
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1580781  1822 VHSqcfVITSDNRYILVCGFWDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSESyigGNcYILSGSRDATLLLW 1895
Cdd:COG2319   81 VLS---VAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPD---GK-TLASGSADGTVRLW 147
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1818-1895 2.36e-04

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: 45.40  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1818 QSIQVHS---QCFVITSDNRYIlVCGFWDKSFRVYSTDTGRLIQVVFGHWDVVTCLArsesYIGGNCYILSGSRDATLLL 1894
Cdd:cd00200  129 TTLRGHTdwvNSVAFSPDGTFV-ASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVA----FSPDGEKLLSSSSDGTIKL 203


                 .
gi 1580781  1895 W 1895
Cdd:cd00200  204 W 204
PH-like cd00900
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1319-1406 8.21e-04

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


Pssm-ID: 275390  Cd Length: 89  Bit Score: 40.07  E-value: 8.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781  1319 VKGTLSVTSSELYFEVDEEDPnfkkidpkilaytegLHGKWLFTEIRSIFSRRYLLQNTALEIFMANRVA-VMFNFPDPA 1397
Cdd:cd00900   16 VEGTLYITSDRLILRDKNDGG---------------LELSIPISDIVNVNVSPQGPSSRYLVLVLKDRGEfVGFSFPKEE 80


                 ....*....
gi 1580781  1398 TVKKVVNFL 1406
Cdd:cd00900   81 DAIEISDAL 89
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1825-1895 1.20e-03

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: 43.09  E-value: 1.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1580781  1825 QCFVITSDNRYILVCGFwDKSFRVYSTDTGRLIQVVFGHWDVVTCLARSESyiggNCYILSGSRDATLLLW 1895
Cdd:cd00200  181 NSVAFSPDGEKLLSSSS-DGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD----GYLLASGSEDGTIRVW 246
motB PRK12799
flagellar motor protein MotB; Reviewed
 858-1021 1.48e-03

flagellar motor protein MotB; Reviewed


Pssm-ID: 183756 [Multi-domain]  Cd Length: 421  Bit Score: 43.17  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    858 AGPDAISEVLSTLSLevNKSPETKNDRGNdLDTKAtpsVSVSKNVNVKDI----LRSLVNIPADGVTVDPALLPPACLGA 933
Cdd:PRK12799  250 ASDDPVNRRISILVL--NKQSQHDIEHEN-LDNRA---LDIEKATGLKQIdthgTVPVAAVTPSSAVTQSSAITPSSAAI 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1580781    934 LGDLSVEQPVQFRSFD--RSVIVAAKKSAVSPSTFNTSI--------PTNAVSVVSSVDSAQASDMGGESPGSRSSNAKL 1003
Cdd:PRK12799  324 PSPAVIPSSVTTQSATttQASAVALSSAGVLPSDVTLPGtvalpaaePVNMQPQPMSTTETQQSSTGNITSTANGPTTSL 403

                         170
                  ....*....|....*...
gi 1580781   1004 PSVPTvdsvSQDPVSNMS 1021
Cdd:PRK12799  404 PAAPA----SNIPVSPTS 417
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1826-1902 2.86e-03

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: 41.94  E-value: 2.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1580781  1826 CFVITSDNRYILVCGfWDKSFRVYSTDTGRLIQVVFGHWDVVTCLArsesYIGGNCYILSGSRDATLLLWYWNGNAV 1902
Cdd:cd00200   14 CVAFSPDGKLLATGS-GDGTIKVWDLETGELLRTLKGHTGPVRDVA----ASADGTYLASGSSDKTIRLWDLETGEC 85
WD40 pfam00400
WD domain, G-beta repeat;
1854-1895 4.41e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 4.41e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1580781    1854 GRLIQVVFGHWDVVTCLARSESyiggNCYILSGSRDATLLLW 1895
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPD----GKLLASGSDDGTVKVW 38
 
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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