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Conserved domains on  [gi|386768401|ref|NP_001246451|]
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mahjong, isoform B [Drosophila melanogaster]

Protein Classification

LisH and WD40 domain-containing protein( domain architecture ID 13922655)

LisH and WD40 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1159-1350 8.41e-11

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: 64.66  E-value: 8.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1159 TCCDLA--GKYIIVGTQQGDGRVFNMNDGvEQFFSNC-HNFSVDAIKANRAGDLVITSSFWRTptSILWSIADDEFKLKL 1235
Cdd:cd00200    13 TCVAFSpdGKLLATGSGDGTIKVWDLETG-ELLRTLKgHTGPVRDVAASADGTYLASGSSDKT--IRLWDLETGECVRTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1236 R--LPDVTYCEFSQTvqDRLL--GTQNECATLFDINTGSKVASFTptipnlyTKNRATLC----RTDELILS---DGV-- 1302
Cdd:cd00200    90 TghTSYVSSVAFSPD--GRILssSSRDKTIKVWDVETGKCLTTLR-------GHTDWVNSvafsPDGTFVASssqDGTik 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386768401 1303 LWDVRSGKEIHKFDKFNQCISGV-FHPNCLEIIANTE-----VWDLRTFHLLQT 1350
Cdd:cd00200   161 LWDLRTGKCVATLTGHTGEVNSVaFSPDGEKLLSSSSdgtikLWDLSTGKCLGT 214
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 912-944 6.00e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


:

Pssm-ID: 128913  Cd Length: 34  Bit Score: 41.27  E-value: 6.00e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 386768401    912 NKQQLYQLIFEHLESNGLSQTAQMLQREVGLPL 944
Cdd:smart00667    2 SRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1159-1350 8.41e-11

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: 64.66  E-value: 8.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1159 TCCDLA--GKYIIVGTQQGDGRVFNMNDGvEQFFSNC-HNFSVDAIKANRAGDLVITSSFWRTptSILWSIADDEFKLKL 1235
Cdd:cd00200    13 TCVAFSpdGKLLATGSGDGTIKVWDLETG-ELLRTLKgHTGPVRDVAASADGTYLASGSSDKT--IRLWDLETGECVRTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1236 R--LPDVTYCEFSQTvqDRLL--GTQNECATLFDINTGSKVASFTptipnlyTKNRATLC----RTDELILS---DGV-- 1302
Cdd:cd00200    90 TghTSYVSSVAFSPD--GRILssSSRDKTIKVWDVETGKCLTTLR-------GHTDWVNSvafsPDGTFVASssqDGTik 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386768401 1303 LWDVRSGKEIHKFDKFNQCISGV-FHPNCLEIIANTE-----VWDLRTFHLLQT 1350
Cdd:cd00200   161 LWDLRTGKCVATLTGHTGEVNSVaFSPDGEKLLSSSSdgtikLWDLSTGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
1165-1423 2.24e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 48.75  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1165 GKYIIVGTQQGDGRVFNMNDGVEQFFSNCHNFSVDAIKANRAGDLVITSSFWRTptsI-LWSIADDEFKLKLRLPD--VT 1241
Cdd:COG2319    90 GRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGT---VrLWDLATGKLLRTLTGHSgaVT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1242 YCEFSQtvQDRLL--GTQNECATLFDINTGSKVASFTPTIPNLytkNRATLCRTDELILS---DGV--LWDVRSGKEIHK 1314
Cdd:COG2319   167 SVAFSP--DGKLLasGSDDGTVRLWDLATGKLLRTLTGHTGAV---RSVAFSPDGKLLASgsaDGTvrLWDLATGKLLRT 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1315 FDKFNQCISGV-FHPNCLEIIANTE-----VWDLRTFHLLQTVPVLDQR--NCTFSPmhviygaslgaDRDHdMETTTYD 1386
Cdd:COG2319   242 LTGHSGSVRSVaFSPDGRLLASGSAdgtvrLWDLATGELLRTLTGHSGGvnSVAFSP-----------DGKL-LASGSDD 309

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 386768401 1387 TSFNVLDAYDYSSIATIDVKRN-INDLSVSANGSLIAV 1423
Cdd:COG2319   310 GTVRLWDLATGKLLRTLTGHTGaVRSVAFSPDGKTLAS 347
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 912-944 6.00e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 41.27  E-value: 6.00e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 386768401    912 NKQQLYQLIFEHLESNGLSQTAQMLQREVGLPL 944
Cdd:smart00667    2 SRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1159-1350 8.41e-11

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: 64.66  E-value: 8.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1159 TCCDLA--GKYIIVGTQQGDGRVFNMNDGvEQFFSNC-HNFSVDAIKANRAGDLVITSSFWRTptSILWSIADDEFKLKL 1235
Cdd:cd00200    13 TCVAFSpdGKLLATGSGDGTIKVWDLETG-ELLRTLKgHTGPVRDVAASADGTYLASGSSDKT--IRLWDLETGECVRTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1236 R--LPDVTYCEFSQTvqDRLL--GTQNECATLFDINTGSKVASFTptipnlyTKNRATLC----RTDELILS---DGV-- 1302
Cdd:cd00200    90 TghTSYVSSVAFSPD--GRILssSSRDKTIKVWDVETGKCLTTLR-------GHTDWVNSvafsPDGTFVASssqDGTik 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386768401 1303 LWDVRSGKEIHKFDKFNQCISGV-FHPNCLEIIANTE-----VWDLRTFHLLQT 1350
Cdd:cd00200   161 LWDLRTGKCVATLTGHTGEVNSVaFSPDGEKLLSSSSdgtikLWDLSTGKCLGT 214
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1141-1352 2.16e-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: 51.18  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1141 HFSPWRSIRSadyedleftCCDlaGKYIIVGTQQGDGRVFNMNDGVEQFFSNCHNFSVDAIKANRAGDLVITSSfwRTPT 1220
Cdd:cd00200    50 HTGPVRDVAA---------SAD--GTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSS--RDKT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1221 SILWSIADDEFKLKLR--LPDVTYCEFSQTvqDRLL--GTQNECATLFDINTGSKVASFTPTIPNLYTknrATLCRTDEL 1296
Cdd:cd00200   117 IKVWDVETGKCLTTLRghTDWVNSVAFSPD--GTFVasSSQDGTIKLWDLRTGKCVATLTGHTGEVNS---VAFSPDGEK 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386768401 1297 IL---SDGV--LWDVRSGKEIHKFDKF-NQCISGVFHPNCLEIIA-----NTEVWDLRTFHLLQTVP 1352
Cdd:cd00200   192 LLsssSDGTikLWDLSTGKCLGTLRGHeNGVNSVAFSPDGYLLASgsedgTIRVWDLRTGECVQTLS 258
WD40 COG2319
WD40 repeat [General function prediction only];
1165-1423 2.24e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 48.75  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1165 GKYIIVGTQQGDGRVFNMNDGVEQFFSNCHNFSVDAIKANRAGDLVITSSFWRTptsI-LWSIADDEFKLKLRLPD--VT 1241
Cdd:COG2319    90 GRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGT---VrLWDLATGKLLRTLTGHSgaVT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1242 YCEFSQtvQDRLL--GTQNECATLFDINTGSKVASFTPTIPNLytkNRATLCRTDELILS---DGV--LWDVRSGKEIHK 1314
Cdd:COG2319   167 SVAFSP--DGKLLasGSDDGTVRLWDLATGKLLRTLTGHTGAV---RSVAFSPDGKLLASgsaDGTvrLWDLATGKLLRT 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1315 FDKFNQCISGV-FHPNCLEIIANTE-----VWDLRTFHLLQTVPVLDQR--NCTFSPmhviygaslgaDRDHdMETTTYD 1386
Cdd:COG2319   242 LTGHSGSVRSVaFSPDGRLLASGSAdgtvrLWDLATGELLRTLTGHSGGvnSVAFSP-----------DGKL-LASGSDD 309

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 386768401 1387 TSFNVLDAYDYSSIATIDVKRN-INDLSVSANGSLIAV 1423
Cdd:COG2319   310 GTVRLWDLATGKLLRTLTGHTGaVRSVAFSPDGKTLAS 347
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 912-944 6.00e-05

Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.


Pssm-ID: 128913  Cd Length: 34  Bit Score: 41.27  E-value: 6.00e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 386768401    912 NKQQLYQLIFEHLESNGLSQTAQMLQREVGLPL 944
Cdd:smart00667    2 SRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
WD40 COG2319
WD40 repeat [General function prediction only];
1165-1350 1.33e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.06  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1165 GKYIIVGTQQGDGRVFNMNDGVEQFFSNCHNFSVDAIKANRAGDLVITSSfwRTPTSILWSIADDEFKLKLRLPD--VTY 1242
Cdd:COG2319   174 GKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGS--ADGTVRLWDLATGKLLRTLTGHSgsVRS 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1243 CEFSQtvQDRLL--GTQNECATLFDINTGSKVASFTPTIPNLytkNRATLCRTDELILS---DGV--LWDVRSGKEIHKF 1315
Cdd:COG2319   252 VAFSP--DGRLLasGSADGTVRLWDLATGELLRTLTGHSGGV---NSVAFSPDGKLLASgsdDGTvrLWDLATGKLLRTL 326

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 386768401 1316 DKFNQCISGV-FHPNCLEIIA----NT-EVWDLRTFHLLQT 1350
Cdd:COG2319   327 TGHTGAVRSVaFSPDGKTLASgsddGTvRLWDLATGELLRT 367
WD40 COG2319
WD40 repeat [General function prediction only];
1165-1344 4.40e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 41.44  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1165 GKYIIVGTQQGDGRVFNMNDGVEQFFSNCHNFSVDAIKANRAGDLVITSSFWRTPTsiLWSIADDEFKLKLRLPD--VTY 1242
Cdd:COG2319   216 GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVR--LWDLATGELLRTLTGHSggVNS 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386768401 1243 CEFSQtvQDRLL------GTqnecATLFDINTGSKVASFTPTIPNLYTknrATLCRTDELILS---DGV--LWDVRSGKE 1311
Cdd:COG2319   294 VAFSP--DGKLLasgsddGT----VRLWDLATGKLLRTLTGHTGAVRS---VAFSPDGKTLASgsdDGTvrLWDLATGEL 364

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 386768401 1312 IHKFDKFNQCISGV-FHPNCLEIIA----NT-EVWDLRT 1344
Cdd:COG2319   365 LRTLTGHTGAVTSVaFSPDGRTLASgsadGTvRLWDLAT 403
 
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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