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Conserved domains on  [gi|386766074|ref|NP_001247189|]
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Smu1 spliceosomal factor, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
203-509 9.96e-70

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 228.64  E-value: 9.96e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 203 TQLFRQIKFGQKSHVECAQFSPDGQYLITGSVDGFLEVWNFTTGKVRKDLKYQaqdqfmmmEQAVLALNFSRDSEMVASG 282
Cdd:COG2319  109 TGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGH--------SGAVTSVAFSPDGKLLASG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 283 AQDGQIKVWRIITGQCLRKFeKAHTKGITCLQFSRDNSQVLSASFDYTVRLHGLKSGKMLKEFKGHSSFVNEATFTPDGH 362
Cdd:COG2319  181 SDDGTVRLWDLATGKLLRTL-TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGR 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 363 SVLSASSDGTVKVWSLKTTECVATYKplGNELAVNTVLILPkNPEHFIVCNRSNTVVIMNMQ-GQIVRSFSSgkrEGGAF 441
Cdd:COG2319  260 LLASGSADGTVRLWDLATGELLRTLT--GHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLAtGKLLRTLTG---HTGAV 333

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386766074 442 ISATLSPRGEFIYCAGEDQVLYCFSVSSGKLERTLNVHEKDVIGLTHHPHQNLLASYSEDGLLKLWKP 509
Cdd:COG2319  334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
LisH_TPL super family cl39307
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
 7-36 1.70e-09

LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif.


The actual alignment was detected with superfamily member pfam17814:

Pssm-ID: 375350  Cd Length: 30  Bit Score: 52.78  E-value: 1.70e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 386766074    7 SADVIRLIQQYLKESNLMKTLQTLQEETGV 36
Cdd:pfam17814   1 SQDVVRLILQFLKENGLHRTLQALQTESGV 30
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 40-90 2.08e-06

C-terminal to LisH motif; Alpha-helical motif of unknown function.


:

Pssm-ID: 128914  Cd Length: 58  Bit Score: 44.87  E-value: 2.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386766074    40 TVDSVDGFVQDISNGHWDTVLKVTQSLKLPDKK-----LLNLYEQIVLELIELREL 90
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLErnsklEFELRKQKFLELVRQGKL 56
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
203-509 9.96e-70

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 228.64  E-value: 9.96e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 203 TQLFRQIKFGQKSHVECAQFSPDGQYLITGSVDGFLEVWNFTTGKVRKDLKYQaqdqfmmmEQAVLALNFSRDSEMVASG 282
Cdd:COG2319  109 TGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGH--------SGAVTSVAFSPDGKLLASG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 283 AQDGQIKVWRIITGQCLRKFeKAHTKGITCLQFSRDNSQVLSASFDYTVRLHGLKSGKMLKEFKGHSSFVNEATFTPDGH 362
Cdd:COG2319  181 SDDGTVRLWDLATGKLLRTL-TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGR 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 363 SVLSASSDGTVKVWSLKTTECVATYKplGNELAVNTVLILPkNPEHFIVCNRSNTVVIMNMQ-GQIVRSFSSgkrEGGAF 441
Cdd:COG2319  260 LLASGSADGTVRLWDLATGELLRTLT--GHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLAtGKLLRTLTG---HTGAV 333

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386766074 442 ISATLSPRGEFIYCAGEDQVLYCFSVSSGKLERTLNVHEKDVIGLTHHPHQNLLASYSEDGLLKLWKP 509
Cdd:COG2319  334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 214-508 3.12e-66

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: 215.66  E-value: 3.12e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 214 KSH---VECAQFSPDGQYLITGSVDGFLEVWNFTTGKVRKDLKYQaqdqfmmmEQAVLALNFSRDSEMVASGAQDGQIKV 290
Cdd:cd00200    6 KGHtggVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGH--------TGPVRDVAASADGTYLASGSSDKTIRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 291 WRIITGQCLRKFEkAHTKGITCLQFSRDNSQVLSASFDYTVRLHGLKSGKMLKEFKGHSSFVNEATFTPDGHSVLSASSD 370
Cdd:cd00200   78 WDLETGECVRTLT-GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 371 GTVKVWSLKTTECVATYKplGNELAVNTVLILPKNpEHFIVCNRSNTVVIMNMQ-GQIVRSFSSgkrEGGAFISATLSPR 449
Cdd:cd00200  157 GTIKLWDLRTGKCVATLT--GHTGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLStGKCLGTLRG---HENGVNSVAFSPD 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386766074 450 GEFIYCAGEDQVLYCFSVSSGKLERTLNVHEKDVIGLTHHPHQNLLASYSEDGLLKLWK 508
Cdd:cd00200  231 GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 184-390 4.42e-11

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 65.49  E-value: 4.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 184 IDLFRGKAAMKDQEEEMYPT-QLFRQIKFGQ-------KSHVECAQFspdgqylitgsvDGFLEVWNFTTGKVRKDLKYQ 255
Cdd:PLN00181 507 IKIFECESIIKDGRDIHYPVvELASRSKLSGicwnsyiKSQVASSNF------------EGVVQVWDVARSQLVTEMKEH 574

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 256 aqdqfmmmEQAVLALNFSR-DSEMVASGAQDGQIKVWRIITGQCLRKFEkahTKG-ITCLQFSRDNSQVLS-ASFDYTVR 332
Cdd:PLN00181 575 --------EKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIK---TKAnICCVQFPSESGRSLAfGSADHKVY 643

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386766074 333 LHGLKSGKM-LKEFKGHSSFVNEATFTpDGHSVLSASSDGTVKVWSLKTTECVATYKPL 390
Cdd:PLN00181 644 YYDLRNPKLpLCTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDLSMSISGINETPL 701
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
 7-36 1.70e-09

LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif.


Pssm-ID: 375350  Cd Length: 30  Bit Score: 52.78  E-value: 1.70e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 386766074    7 SADVIRLIQQYLKESNLMKTLQTLQEETGV 36
Cdd:pfam17814   1 SQDVVRLILQFLKENGLHRTLQALQTESGV 30
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 338-377 4.47e-09

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: 51.93  E-value: 4.47e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 386766074   338 SGKMLKEFKGHSSFVNEATFTPDGHSVLSASSDGTVKVWS 377
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
339-377 1.20e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.81  E-value: 1.20e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 386766074  339 GKMLKEFKGHSSFVNEATFTPDGHSVLSASSDGTVKVWS 377
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 40-90 2.08e-06

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 44.87  E-value: 2.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386766074    40 TVDSVDGFVQDISNGHWDTVLKVTQSLKLPDKK-----LLNLYEQIVLELIELREL 90
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLErnsklEFELRKQKFLELVRQGKL 56
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 5-38 1.66e-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: 41.65  E-value: 1.66e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 386766074     5 IESADVIRLIQQYLKESNLMKTLQTLQEETGVSL 38
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
203-509 9.96e-70

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 228.64  E-value: 9.96e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 203 TQLFRQIKFGQKSHVECAQFSPDGQYLITGSVDGFLEVWNFTTGKVRKDLKYQaqdqfmmmEQAVLALNFSRDSEMVASG 282
Cdd:COG2319  109 TGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGH--------SGAVTSVAFSPDGKLLASG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 283 AQDGQIKVWRIITGQCLRKFeKAHTKGITCLQFSRDNSQVLSASFDYTVRLHGLKSGKMLKEFKGHSSFVNEATFTPDGH 362
Cdd:COG2319  181 SDDGTVRLWDLATGKLLRTL-TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGR 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 363 SVLSASSDGTVKVWSLKTTECVATYKplGNELAVNTVLILPkNPEHFIVCNRSNTVVIMNMQ-GQIVRSFSSgkrEGGAF 441
Cdd:COG2319  260 LLASGSADGTVRLWDLATGELLRTLT--GHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLAtGKLLRTLTG---HTGAV 333

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386766074 442 ISATLSPRGEFIYCAGEDQVLYCFSVSSGKLERTLNVHEKDVIGLTHHPHQNLLASYSEDGLLKLWKP 509
Cdd:COG2319  334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 214-508 3.12e-66

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: 215.66  E-value: 3.12e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 214 KSH---VECAQFSPDGQYLITGSVDGFLEVWNFTTGKVRKDLKYQaqdqfmmmEQAVLALNFSRDSEMVASGAQDGQIKV 290
Cdd:cd00200    6 KGHtggVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGH--------TGPVRDVAASADGTYLASGSSDKTIRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 291 WRIITGQCLRKFEkAHTKGITCLQFSRDNSQVLSASFDYTVRLHGLKSGKMLKEFKGHSSFVNEATFTPDGHSVLSASSD 370
Cdd:cd00200   78 WDLETGECVRTLT-GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 371 GTVKVWSLKTTECVATYKplGNELAVNTVLILPKNpEHFIVCNRSNTVVIMNMQ-GQIVRSFSSgkrEGGAFISATLSPR 449
Cdd:cd00200  157 GTIKLWDLRTGKCVATLT--GHTGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLStGKCLGTLRG---HENGVNSVAFSPD 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386766074 450 GEFIYCAGEDQVLYCFSVSSGKLERTLNVHEKDVIGLTHHPHQNLLASYSEDGLLKLWK 508
Cdd:cd00200  231 GYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
212-507 2.70e-62

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 209.00  E-value: 2.70e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 212 GQKSHVECAQFSPDGQYLITGSVDGFLEVWNFTTGKVRKDLKYQaqdqfmmmEQAVLALNFSRDSEMVASGAQDGQIKVW 291
Cdd:COG2319   76 GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGH--------TGAVRSVAFSPDGKTLASGSADGTVRLW 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 292 RIITGQCLRKFeKAHTKGITCLQFSRDNSQVLSASFDYTVRLHGLKSGKMLKEFKGHSSFVNEATFTPDGHSVLSASSDG 371
Cdd:COG2319  148 DLATGKLLRTL-TGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADG 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 372 TVKVWSLKTTECVATYKplGNELAVNTVLILPKNpEHFIVCNRSNTVVIMNMQ-GQIVRSFSSgkrEGGAFISATLSPRG 450
Cdd:COG2319  227 TVRLWDLATGKLLRTLT--GHSGSVRSVAFSPDG-RLLASGSADGTVRLWDLAtGELLRTLTG---HSGGVNSVAFSPDG 300

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 386766074 451 EFIYCAGEDQVLYCFSVSSGKLERTLNVHEKDVIGLTHHPHQNLLASYSEDGLLKLW 507
Cdd:COG2319  301 KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLW 357
WD40 COG2319
WD40 repeat [General function prediction only];
212-507 1.78e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 180.11  E-value: 1.78e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 212 GQKSHVECAQFSPDGQYLITGSVDGFLEVWNFTTGKVRKDLKYQAQdqfmmmeqAVLALNFSRDSEMVASGAQDGQIKVW 291
Cdd:COG2319   34 GLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA--------AVLSVAFSPDGRLLASASADGTVRLW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 292 RIITGQCLRKFEkAHTKGITCLQFSRDNSQVLSASFDYTVRLHGLKSGKMLKEFKGHSSFVNEATFTPDGHSVLSASSDG 371
Cdd:COG2319  106 DLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 372 TVKVWSLKTTECVATYKplGNELAVNTVLILPKNpEHFIVCNRSNTVVIMNMQ-GQIVRSFssgKREGGAFISATLSPRG 450
Cdd:COG2319  185 TVRLWDLATGKLLRTLT--GHTGAVRSVAFSPDG-KLLASGSADGTVRLWDLAtGKLLRTL---TGHSGSVRSVAFSPDG 258

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 386766074 451 EFIYCAGEDQVLYCFSVSSGKLERTLNVHEKDVIGLTHHPHQNLLASYSEDGLLKLW 507
Cdd:COG2319  259 RLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW 315
WD40 COG2319
WD40 repeat [General function prediction only];
212-380 1.06e-45

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 164.70  E-value: 1.06e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 212 GQKSHVECAQFSPDGQYLITGSVDGFLEVWNFTTGKVRKDLKYQaqdqfmmmEQAVLALNFSRDSEMVASGAQDGQIKVW 291
Cdd:COG2319  244 GHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH--------SGGVNSVAFSPDGKLLASGSDDGTVRLW 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 292 RIITGQCLRKFeKAHTKGITCLQFSRDNSQVLSASFDYTVRLHGLKSGKMLKEFKGHSSFVNEATFTPDGHSVLSASSDG 371
Cdd:COG2319  316 DLATGKLLRTL-TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADG 394


                 ....*....
gi 386766074 372 TVKVWSLKT 380
Cdd:COG2319  395 TVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 212-406 2.06e-44

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: 157.88  E-value: 2.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 212 GQKSHVECAQFSPDGQYLITGSVDGFLEVWNFTTGKVRKDLKYQaqdqfmmmEQAVLALNFSRDSEMVASGAQDGQIKVW 291
Cdd:cd00200   91 GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH--------TDWVNSVAFSPDGTFVASSSQDGTIKLW 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 292 RIITGQCLRKFEkAHTKGITCLQFSRDNSQVLSASFDYTVRLHGLKSGKMLKEFKGHSSFVNEATFTPDGHSVLSASSDG 371
Cdd:cd00200  163 DLRTGKCVATLT-GHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDG 241

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 386766074 372 TVKVWSLKTTECVATYKplGNELAVNTVLILPKNP 406
Cdd:cd00200  242 TIRVWDLRTGECVQTLS--GHTNSVTSLAWSPDGK 274
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 341-507 2.20e-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: 97.02  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 341 MLKEFKGHSSFVNEATFTPDGHSVLSASSDGTVKVWSLKTTECVATYKplGNELAVNTVLILPKNPEhFIVCNRSNTVVI 420
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK--GHTGPVRDVAASADGTY-LASGSSDKTIRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 421 MNMQ-GQIVRSFssgkrEG--GAFISATLSPRGEFIYCAGEDQVLYCFSVSSGKLERTLNVHEKDVIGLTHHPHQNLLAS 497
Cdd:cd00200   78 WDLEtGECVRTL-----TGhtSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVAS 152

                        170
                 ....*....|
gi 386766074 498 YSEDGLLKLW 507
Cdd:cd00200  153 SSQDGTIKLW 162
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 184-390 4.42e-11

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 65.49  E-value: 4.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 184 IDLFRGKAAMKDQEEEMYPT-QLFRQIKFGQ-------KSHVECAQFspdgqylitgsvDGFLEVWNFTTGKVRKDLKYQ 255
Cdd:PLN00181 507 IKIFECESIIKDGRDIHYPVvELASRSKLSGicwnsyiKSQVASSNF------------EGVVQVWDVARSQLVTEMKEH 574

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 256 aqdqfmmmEQAVLALNFSR-DSEMVASGAQDGQIKVWRIITGQCLRKFEkahTKG-ITCLQFSRDNSQVLS-ASFDYTVR 332
Cdd:PLN00181 575 --------EKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIK---TKAnICCVQFPSESGRSLAfGSADHKVY 643

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386766074 333 LHGLKSGKM-LKEFKGHSSFVNEATFTpDGHSVLSASSDGTVKVWSLKTTECVATYKPL 390
Cdd:PLN00181 644 YYDLRNPKLpLCTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDLSMSISGINETPL 701
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
 7-36 1.70e-09

LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal domain containing a lissencephaly homologous (LisH) dimerization motif.


Pssm-ID: 375350  Cd Length: 30  Bit Score: 52.78  E-value: 1.70e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 386766074    7 SADVIRLIQQYLKESNLMKTLQTLQEETGV 36
Cdd:pfam17814   1 SQDVVRLILQFLKENGLHRTLQALQTESGV 30
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 338-377 4.47e-09

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: 51.93  E-value: 4.47e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 386766074   338 SGKMLKEFKGHSSFVNEATFTPDGHSVLSASSDGTVKVWS 377
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
339-377 1.20e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.81  E-value: 1.20e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 386766074  339 GKMLKEFKGHSSFVNEATFTPDGHSVLSASSDGTVKVWS 377
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 232-392 1.27e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 54.32  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 232 GSVDGFLE----VWNFTTGKVRKDLKyqaQDQFMMMEQAVLALNFSRDSEMVASGAQDGQIKVW---------RIITGQC 298
Cdd:PLN00181 450 GWIDPFLEglckYLSFSKLRVKADLK---QGDLLNSSNLVCAIGFDRDGEFFATAGVNKKIKIFecesiikdgRDIHYPV 526

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074 299 LRKFEKAHTKGItCLQfSRDNSQVLSASFDYTVRLHGLKSGKMLKEFKGHSSFVNEATFTPDGHSVL-SASSDGTVKVWS 377
Cdd:PLN00181 527 VELASRSKLSGI-CWN-SYIKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLaSGSDDGSVKLWS 604

                        170
                 ....*....|....*
gi 386766074 378 LKTTECVATYKPLGN 392
Cdd:PLN00181 605 INQGVSIGTIKTKAN 619
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 295-334 5.54e-07

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: 46.15  E-value: 5.54e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 386766074   295 TGQCLRKFeKAHTKGITCLQFSRDNSQVLSASFDYTVRLH 334
Cdd:smart00320   1 SGELLKTL-KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 40-90 2.08e-06

C-terminal to LisH motif; Alpha-helical motif of unknown function.


Pssm-ID: 128914  Cd Length: 58  Bit Score: 44.87  E-value: 2.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386766074    40 TVDSVDGFVQDISNGHWDTVLKVTQSLKLPDKK-----LLNLYEQIVLELIELREL 90
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLErnsklEFELRKQKFLELVRQGKL 56
WD40 pfam00400
WD domain, G-beta repeat;
296-333 5.53e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.10  E-value: 5.53e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386766074  296 GQCLRKFeKAHTKGITCLQFSRDNSQVLSASFDYTVRL 333
Cdd:pfam00400   1 GKLLKTL-EGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 469-508 5.83e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 43.07  E-value: 5.83e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 386766074   469 SGKLERTLNVHEKDVIGLTHHPHQNLLASYSEDGLLKLWK 508
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 5-38 1.66e-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: 41.65  E-value: 1.66e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 386766074     5 IESADVIRLIQQYLKESNLMKTLQTLQEETGVSL 38
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 212-242 2.28e-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: 41.53  E-value: 2.28e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 386766074   212 GQKSHVECAQFSPDGQYLITGSVDGFLEVWN 242
Cdd:smart00320  10 GHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
470-507 3.98e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 3.98e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 386766074  470 GKLERTLNVHEKDVIGLTHHPHQNLLASYSEDGLLKLW 507
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 pfam00400
WD domain, G-beta repeat;
212-242 4.47e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 4.47e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 386766074  212 GQKSHVECAQFSPDGQYLITGSVDGFLEVWN 242
Cdd:pfam00400   9 GHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 264-291 5.57e-04

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: 37.68  E-value: 5.57e-04
                           10        20
                   ....*....|....*....|....*...
gi 386766074   264 EQAVLALNFSRDSEMVASGAQDGQIKVW 291
Cdd:smart00320  12 TGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
264-291 9.81e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 9.81e-04
                          10        20
                  ....*....|....*....|....*...
gi 386766074  264 EQAVLALNFSRDSEMVASGAQDGQIKVW 291
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVW 38
Nup160 pfam11715
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
 350-416 2.60e-03

Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous with the Nup160 of vertebrates. The nuclear core complex, or NPC, mediates macromolecular transport across the nuclear envelope. Deletion of the NUP120 gene causes clustering of NPCs at one side of the nuclear envelope, moderate nucleolar fragmentation and slower cell growth. The vertebrate NPC is estimated to contain between 30 and 60 different proteins. most of which are not known. Two important ones in creating the nucleoporin basket are Nup98 and Nup153, and Nup120, in conjunction with Nup 133, interacts with these two and itself plays a role in mRNA export. Nup160, Nup133, Nup96, and Nup107 are all targets of phosphorylation. The phosphorylation sites are clustered mainly at the N-terminal regions of these proteins, which are predicted to be natively disordered. The entire Nup107-160 sub-complex is stable throughout the cell cycle, thus it seems unlikely that phosphorylation affects interactions within the Nup107-160 sub-complex, but rather that it regulates the association of the sub-complex with the NPC and other proteins.


Pssm-ID: 432020 [Multi-domain]  Cd Length: 540  Bit Score: 40.52  E-value: 2.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766074  350 SFVNEATFTPDGHSVLSASSDGTVKVWSLKTTECVATYKPLGNELAVNTVLILPKNPEH--FIVCNRSN 416
Cdd:pfam11715 223 SAAPAVTTVGGQNFLFTLSLDHTLRVWDLLTGKCLATIDLLDLELPQDSSSWLTLDPAPssLIRVSGSF 291
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 214-429 3.19e-03

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: 39.67  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074  214 KSHVECAQFSPDGQYLITGSVDGFLEVW-----NFTTGKVRKDLKYQAQDQFMMMEQ----------AVLALNFSRDSEM 278
Cdd:pfam20426 124 KDVVSCVAVTSDGSILATGSYDTTVMVWevlrgRSSEKRSRNTQTEFPRKDHVIAETpfhilcghddIITCLYVSVELDI 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766074  279 VASGAQDGQIKVWRIITGQCLRKFEKAHTKGITCLQFSRDNSQVLSASFDYTVRLHGLkSGKMLK--EFKGHssfVNEAT 356
Cdd:pfam20426 204 VISGSKDGTCIFHTLREGRYVRSIRHPSGCPLSKLVASRHGRIVLYADDDLSLHLYSI-NGKHIAssESNGR---LNCIE 279

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386766074  357 FTPDGHSVLSASSDGTVKVWSLKTTECVATYKPLGNelAVNTVLILPKnpEHFIVCNRSNTVVIMNMQGQIVR 429
Cdd:pfam20426 280 LSSCGEFLVCAGDQGQIVVRSMNSLEVVRRYNGIGK--IITSLTVTPE--ECFLAGTKDGSLLVYSIENPQLR 348
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 472-508 4.46e-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: 39.24  E-value: 4.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 386766074 472 LERTLNVHEKDVIGLTHHPHQNLLASYSEDGLLKLWK 508
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD 37
 
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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