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Conserved domains on  [gi|1026594095|gb|OAD78498|]
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hypothetical protein PHYBLDRAFT_176837 [Phycomyces blakesleeanus NRRL 1555(-)]

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];
214-507 2.14e-54

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 188.20  E-value: 2.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 214 CAVFSPNGQYIATGTVDGFIEIWNYLTGKLRKDLSyqaedslmAMDNAVLCLAFSQDSELLVSGSTDGKITVWKVQTGIS 293
Cdd:COG2319   125 SVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT--------GHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKL 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 294 QRRLsPAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWDT 373
Cdd:COG2319   197 LRTL-TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 374 KTTSCLHTVTPKTNAdlskgalnpvggigsqtVQSIVRVPRNmDQVLICVKSNTLYIMTMR-GQITKSYSHHkktGSDFV 452
Cdd:COG2319   276 ATGELLRTLTGHSGG-----------------VNSVAFSPDG-KLLASGSDDGTVRLWDLAtGKLLRTLTGH---TGAVR 334

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1026594095 453 SAAMSPQGEFVYGVGEDSSLYCFQTTTGNLLGETKIGDAEVIGLVGHPFSNVLAS 507
Cdd:COG2319   335 SVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
 6-35 3.06e-11

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: 57.79  E-value: 3.06e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 1026594095   6 SKDTVKLILQFLRENNLHRTLQALEDESSV 35
Cdd:pfam17814   1 SQDVVRLILQFLKENGLHRTLQALQTESGV 30
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
214-507 2.14e-54

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 188.20  E-value: 2.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 214 CAVFSPNGQYIATGTVDGFIEIWNYLTGKLRKDLSyqaedslmAMDNAVLCLAFSQDSELLVSGSTDGKITVWKVQTGIS 293
Cdd:COG2319   125 SVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT--------GHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKL 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 294 QRRLsPAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWDT 373
Cdd:COG2319   197 LRTL-TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 374 KTTSCLHTVTPKTNAdlskgalnpvggigsqtVQSIVRVPRNmDQVLICVKSNTLYIMTMR-GQITKSYSHHkktGSDFV 452
Cdd:COG2319   276 ATGELLRTLTGHSGG-----------------VNSVAFSPDG-KLLASGSDDGTVRLWDLAtGKLLRTLTGH---TGAVR 334

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1026594095 453 SAAMSPQGEFVYGVGEDSSLYCFQTTTGNLLGETKIGDAEVIGLVGHPFSNVLAS 507
Cdd:COG2319   335 SVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 214-507 2.39e-45

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: 160.58  E-value: 2.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 214 CAVFSPNGQYIATGTVDGFIEIWNYLTGKLrkdlsyqaEDSLMAMDNAVLCLAFSQDSELLVSGSTDGKITVWKVQTGIS 293
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGEL--------LRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGEC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 294 QRRLSpAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWDT 373
Cdd:cd00200    86 VRTLT-GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 374 KTTSCLHTVTPKTNAdlskgalnpvggigsqtVQSIVRVPRNMdQVLICVKSNTLYIMTMR-GQITKSYSHHKKTgsdFV 452
Cdd:cd00200   165 RTGKCVATLTGHTGE-----------------VNSVAFSPDGE-KLLSSSSDGTIKLWDLStGKCLGTLRGHENG---VN 223

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1026594095 453 SAAMSPQGEFVYGVGEDSSLYCFQTTTGNLLGETKIGDAEVIGLVGHPFSNVLAS 507
Cdd:cd00200   224 SVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS 278
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 224-387 2.98e-12

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 69.35  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 224 IATGTVDGFIEIWNYLTGKLRKDLSyQAEDSLMAMDNAvlclafSQDSELLVSGSTDGKITVWKVQTGISQRRLSPahSQ 303
Cdd:PLN00181  548 VASSNFEGVVQVWDVARSQLVTEMK-EHEKRVWSIDYS------SADPTLLASGSDDGSVKLWSINQGVSIGTIKT--KA 618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 304 GVTSVCFNKDGTQVLS-GSYDHTVKIHGLKSGKT-LKEFRGHSSFVNAVAFsSDYTRVLSASSDGTVKIWDTKTT----- 376
Cdd:PLN00181  619 NICCVQFPSESGRSLAfGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRF-VDSSTLVSSSTDNTLKLWDLSMSisgin 697

                         170
                  ....*....|..
gi 1026594095 377 -SCLHTVTPKTN 387
Cdd:PLN00181  698 eTPLHSFMGHTN 709
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
 6-35 3.06e-11

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: 57.79  E-value: 3.06e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 1026594095   6 SKDTVKLILQFLRENNLHRTLQALEDESSV 35
Cdd:pfam17814   1 SQDVVRLILQFLKENGLHRTLQALQTESGV 30
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 333-372 8.11e-11

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: 56.94  E-value: 8.11e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1026594095  333 SGKTLKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWD 372
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
334-372 3.40e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 3.40e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1026594095 334 GKTLKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWD 372
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 4-37 1.35e-04

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: 38.95  E-value: 1.35e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1026594095    4 VQSKDTVKLILQFLRENNLHRTLQALEDESSVTL 37
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
214-507 2.14e-54

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 188.20  E-value: 2.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 214 CAVFSPNGQYIATGTVDGFIEIWNYLTGKLRKDLSyqaedslmAMDNAVLCLAFSQDSELLVSGSTDGKITVWKVQTGIS 293
Cdd:COG2319   125 SVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT--------GHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKL 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 294 QRRLsPAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWDT 373
Cdd:COG2319   197 LRTL-TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 374 KTTSCLHTVTPKTNAdlskgalnpvggigsqtVQSIVRVPRNmDQVLICVKSNTLYIMTMR-GQITKSYSHHkktGSDFV 452
Cdd:COG2319   276 ATGELLRTLTGHSGG-----------------VNSVAFSPDG-KLLASGSDDGTVRLWDLAtGKLLRTLTGH---TGAVR 334

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1026594095 453 SAAMSPQGEFVYGVGEDSSLYCFQTTTGNLLGETKIGDAEVIGLVGHPFSNVLAS 507
Cdd:COG2319   335 SVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
WD40 COG2319
WD40 repeat [General function prediction only];
205-401 4.45e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 176.64  E-value: 4.45e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 205 FPGKKTFAECAVFSPNGQYIATGTVDGFIEIWNYLTGKLRKDLSyqaedslmAMDNAVLCLAFSQDSELLVSGSTDGKIT 284
Cdd:COG2319   158 LTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT--------GHTGAVRSVAFSPDGKLLASGSADGTVR 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 285 VWKVQTGISQRRLsPAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSSDYTRVLSASS 364
Cdd:COG2319   230 LWDLATGKLLRTL-TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSD 308

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1026594095 365 DGTVKIWDTKTTSCLHTVTPKTNADLSkGALNPVGGI 401
Cdd:COG2319   309 DGTVRLWDLATGKLLRTLTGHTGAVRS-VAFSPDGKT 344
WD40 COG2319
WD40 repeat [General function prediction only];
205-383 8.00e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 173.56  E-value: 8.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 205 FPGKKTFAECAVFSPNGQYIATGTVDGFIEIWNYLTGKLRKDLSYQaedslmamDNAVLCLAFSQDSELLVSGSTDGKIT 284
Cdd:COG2319   200 LTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGH--------SGSVRSVAFSPDGRLLASGSADGTVR 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 285 VWKVQTGiSQRRLSPAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSSDYTRVLSASS 364
Cdd:COG2319   272 LWDLATG-ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSD 350

                         170
                  ....*....|....*....
gi 1026594095 365 DGTVKIWDTKTTSCLHTVT 383
Cdd:COG2319   351 DGTVRLWDLATGELLRTLT 369
WD40 COG2319
WD40 repeat [General function prediction only];
205-375 4.24e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 168.94  E-value: 4.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 205 FPGKKTFAECAVFSPNGQYIATGTVDGFIEIWNYLTGKLRKDLSYQaedslmamDNAVLCLAFSQDSELLVSGSTDGKIT 284
Cdd:COG2319   242 LTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH--------SGGVNSVAFSPDGKLLASGSDDGTVR 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 285 VWKVQTGISQRRLSpAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSSDYTRVLSASS 364
Cdd:COG2319   314 LWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSA 392

                         170
                  ....*....|.
gi 1026594095 365 DGTVKIWDTKT 375
Cdd:COG2319   393 DGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 214-507 2.39e-45

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: 160.58  E-value: 2.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 214 CAVFSPNGQYIATGTVDGFIEIWNYLTGKLrkdlsyqaEDSLMAMDNAVLCLAFSQDSELLVSGSTDGKITVWKVQTGIS 293
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGEL--------LRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGEC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 294 QRRLSpAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWDT 373
Cdd:cd00200    86 VRTLT-GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 374 KTTSCLHTVTPKTNAdlskgalnpvggigsqtVQSIVRVPRNMdQVLICVKSNTLYIMTMR-GQITKSYSHHKKTgsdFV 452
Cdd:cd00200   165 RTGKCVATLTGHTGE-----------------VNSVAFSPDGE-KLLSSSSDGTIKLWDLStGKCLGTLRGHENG---VN 223

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1026594095 453 SAAMSPQGEFVYGVGEDSSLYCFQTTTGNLLGETKIGDAEVIGLVGHPFSNVLAS 507
Cdd:cd00200   224 SVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS 278
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 216-472 4.49e-42

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: 152.10  E-value: 4.49e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 216 VFSPNGQYIATGTVDGFIEIWNYLTGKLRKdlsyqaedSLMAMDNAVLCLAFSQDSELLVSGSTDGKITVWKVQTGISQR 295
Cdd:cd00200    58 AASADGTYLASGSSDKTIRLWDLETGECVR--------TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLT 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 296 RLsPAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWDTKT 375
Cdd:cd00200   130 TL-RGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 376 TSCLHTVTPKTNAdlskgalnpvggigsqtVQSIVRVPrnmDQVLICVKS--NTLYIM-TMRGQITKSYSHHKKTGSdfv 452
Cdd:cd00200   209 GKCLGTLRGHENG-----------------VNSVAFSP---DGYLLASGSedGTIRVWdLRTGECVQTLSGHTNSVT--- 265

                         250       260
                  ....*....|....*....|
gi 1026594095 453 SAAMSPQGEFVYGVGEDSSL 472
Cdd:cd00200   266 SLAWSPDGKRLASGSADGTI 285
WD40 COG2319
WD40 repeat [General function prediction only];
215-514 5.07e-41

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 152.37  E-value: 5.07e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 215 AVFSPNGQYIATGTVDGFIEIWNYLTGKLRKDLSYQaedslmamDNAVLCLAFSQDSELLVSGSTDGKITVWKVQTGISQ 294
Cdd:COG2319    42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH--------TAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 295 RRLSpAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWDTK 374
Cdd:COG2319   114 RTLT-GHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 375 TTSCLHTVTPKTNADLSkGALNPVGGI---GS--QTVQsivrvprnmdqvLICVKSntlyimtmrGQITKSYSHHkktgS 449
Cdd:COG2319   193 TGKLLRTLTGHTGAVRS-VAFSPDGKLlasGSadGTVR------------LWDLAT---------GKLLRTLTGH----S 246

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1026594095 450 DFV-SAAMSPQGEFVYGVGEDSSLYCFQTTTGNLLGETKIGDAEVIGLVGHPFSNVLASYDESGHV 514
Cdd:COG2319   247 GSVrSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTV 312
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 195-372 2.60e-38

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: 141.70  E-value: 2.60e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 195 SVTKPYLSIKFPGKKTFAECAVFSPNGQYIATGTVDGFIEIWNYLTGKLRKDLSyqaedslmAMDNAVLCLAFSQDSELL 274
Cdd:cd00200   121 DVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLT--------GHTGEVNSVAFSPDGEKL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 275 VSGSTDGKITVWKVQTGISQRRLSpAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSS 354
Cdd:cd00200   193 LSSSSDGTIKLWDLSTGKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSP 271

                         170
                  ....*....|....*...
gi 1026594095 355 DYTRVLSASSDGTVKIWD 372
Cdd:cd00200   272 DGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 260-516 4.75e-38

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: 140.93  E-value: 4.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 260 NAVLCLAFSQDSELLVSGSTDGKITVWKVQTGISQRRLSpAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKE 339
Cdd:cd00200    10 GGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK-GHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 340 FRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWDTKTTSCLHTVTPKTNadlskgalnpvggigsqTVQSiVRVPRNMDQV 419
Cdd:cd00200    89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD-----------------WVNS-VAFSPDGTFV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 420 LICVKSNTLYIMTMR-GQITKSYSHHKKTGSdfvSAAMSPQGEFVYGVGEDSSLYCFQTTTGNLLGETKIGDAEVIGLVG 498
Cdd:cd00200   151 ASSSQDGTIKLWDLRtGKCVATLTGHTGEVN---SVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAF 227

                         250
                  ....*....|....*...
gi 1026594095 499 HPFSNVLASYDESGHVYF 516
Cdd:cd00200   228 SPDGYLLASGSEDGTIRV 245
WD40 COG2319
WD40 repeat [General function prediction only];
266-514 1.04e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.10  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 266 AFSQDSELLVSGSTDGKITVWKVQTGISQRRLsPAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSS 345
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLL-LGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 346 FVNAVAFSSDYTRVLSASSDGTVKIWDTKTTSCLHTVTPKTNADLSkGALNPVGgigsqtvqsivrvprnmdQVLICV-K 424
Cdd:COG2319    80 AVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRS-VAFSPDG------------------KTLASGsA 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 425 SNTLYIMTMR-GQITKSYSHHkktgSDFV-SAAMSPQGEFVYGVGEDSSLYCFQTTTGNLLGETKIGDAEVIGLVGHPFS 502
Cdd:COG2319   141 DGTVRLWDLAtGKLLRTLTGH----SGAVtSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDG 216

                         250
                  ....*....|..
gi 1026594095 503 NVLASYDESGHV 514
Cdd:COG2319   217 KLLASGSADGTV 228
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 337-519 6.29e-13

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: 69.29  E-value: 6.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 337 LKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWDTKTTSCLHTVTPKTnadlskgalnpvggigsQTVQSIVRVPRNm 416
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHT-----------------GPVRDVAASADG- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 417 DQVLICVKSNTLYIM-TMRGQITKSYSHHKKTGSdfvSAAMSPQGEFVYGVGEDSSLYCFQTTTGNLLGETKIGDAEVIG 495
Cdd:cd00200    64 TYLASGSSDKTIRLWdLETGECVRTLTGHTSYVS---SVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS 140

                         170       180
                  ....*....|....*....|....*.
gi 1026594095 496 LVGHPFSNVLA--SYDESGHVYFLKA 519
Cdd:cd00200   141 VAFSPDGTFVAssSQDGTIKLWDLRT 166
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 224-387 2.98e-12

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 69.35  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 224 IATGTVDGFIEIWNYLTGKLRKDLSyQAEDSLMAMDNAvlclafSQDSELLVSGSTDGKITVWKVQTGISQRRLSPahSQ 303
Cdd:PLN00181  548 VASSNFEGVVQVWDVARSQLVTEMK-EHEKRVWSIDYS------SADPTLLASGSDDGSVKLWSINQGVSIGTIKT--KA 618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 304 GVTSVCFNKDGTQVLS-GSYDHTVKIHGLKSGKT-LKEFRGHSSFVNAVAFsSDYTRVLSASSDGTVKIWDTKTT----- 376
Cdd:PLN00181  619 NICCVQFPSESGRSLAfGSADHKVYYYDLRNPKLpLCTMIGHSKTVSYVRF-VDSSTLVSSSTDNTLKLWDLSMSisgin 697

                         170
                  ....*....|..
gi 1026594095 377 -SCLHTVTPKTN 387
Cdd:PLN00181  698 eTPLHSFMGHTN 709
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
 6-35 3.06e-11

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: 57.79  E-value: 3.06e-11
                          10        20        30
                  ....*....|....*....|....*....|
gi 1026594095   6 SKDTVKLILQFLRENNLHRTLQALEDESSV 35
Cdd:pfam17814   1 SQDVVRLILQFLKENGLHRTLQALQTESGV 30
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 333-372 8.11e-11

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: 56.94  E-value: 8.11e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1026594095  333 SGKTLKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWD 372
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 227-387 1.97e-10

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 63.57  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 227 GTVDGFIE-IWNYLT-GKLRKDLSYQAEDsLMAMDNAVLCLAFSQDSELLVSGSTDGKITVWKVQTGISQRR------LS 298
Cdd:PLN00181  450 GWIDPFLEgLCKYLSfSKLRVKADLKQGD-LLNSSNLVCAIGFDRDGEFFATAGVNKKIKIFECESIIKDGRdihypvVE 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 299 PAHSQGVTSVCFNKD-GTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSSFVNAVAFSS-DYTRVLSASSDGTVKIWDTKTT 376
Cdd:PLN00181  529 LASRSKLSGICWNSYiKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQG 608

                         170
                  ....*....|.
gi 1026594095 377 SCLHTVTPKTN 387
Cdd:PLN00181  609 VSIGTIKTKAN 619
WD40 pfam00400
WD domain, G-beta repeat;
334-372 3.40e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 3.40e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1026594095 334 GKTLKEFRGHSSFVNAVAFSSDYTRVLSASSDGTVKIWD 372
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 299-329 2.99e-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: 43.84  E-value: 2.99e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1026594095  299 PAHSQGVTSVCFNKDGTQVLSGSYDHTVKIH 329
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 254-287 5.95e-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: 5.95e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1026594095  254 SLMAMDNAVLCLAFSQDSELLVSGSTDGKITVWK 287
Cdd:smart00320   7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
299-328 7.71e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.72  E-value: 7.71e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1026594095 299 PAHSQGVTSVCFNKDGTQVLSGSYDHTVKI 328
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
WD40 pfam00400
WD domain, G-beta repeat;
259-286 5.83e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 5.83e-05
                          10        20
                  ....*....|....*....|....*...
gi 1026594095 259 DNAVLCLAFSQDSELLVSGSTDGKITVW 286
Cdd:pfam00400  11 TGSVTSLAFSPDGKLLASGSDDGTVKVW 38
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 4-37 1.35e-04

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: 38.95  E-value: 1.35e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1026594095    4 VQSKDTVKLILQFLRENNLHRTLQALEDESSVTL 37
Cdd:smart00667   1 ISRSELNRLILEYLLRNGYEETAETLQKESGLSL 34
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 265-355 9.49e-04

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 38.41  E-value: 9.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 265 LAFSQDSELLVSGSTDGKITV----WKVQTGISQrrlsPAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEF 340
Cdd:pfam12894   1 MSWCPTMDLIALATEDGELLLhrlnWQRVWTLSP----DKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHF 76

                          90
                  ....*....|....*
gi 1026594095 341 RGHSSFVNAVAFSSD 355
Cdd:pfam12894  77 SAGSDLITCLGWGEN 91
Nup160 pfam11715
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
 299-381 1.76e-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: 40.91  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 299 PAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLK-----SGKTLKEFRGHS-----SFVNAVAFSSDYTRVLSASSDGTV 368
Cdd:pfam11715 167 SLADGGLLKLTRSSDGGAWKESTFEPASWLQSLSgllgwLADPTIRYSGSSvalslSAAPAVTTVGGQNFLFTLSLDHTL 246

                          90
                  ....*....|...
gi 1026594095 369 KIWDTKTTSCLHT 381
Cdd:pfam11715 247 RVWDLLTGKCLAT 259
PTZ00421 PTZ00421
coronin; Provisional
 217-382 3.04e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 40.26  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 217 FSP-NGQYIATGTVDGFIEIWNYLTGKLRKDLSYQAEDsLMAMDNAVLCLAFSQDSE-LLVSGSTDGKITVWKVQTGISQ 294
Cdd:PTZ00421   83 FNPfDPQKLFTASEDGTIMGWGIPEEGLTQNISDPIVH-LQGHTKKVGIVSFHPSAMnVLASAGADMVVNVWDVERGKAV 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026594095 295 RRLSpAHSQGVTSVCFNKDGTQVLSGSYDHTVKIHGLKSGKTLKEFRGHSS-------------FVNAVAFSSDYTRvls 361
Cdd:PTZ00421  162 EVIK-CHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHASaksqrclwakrkdLIITLGCSKSQQR--- 237

                         170       180
                  ....*....|....*....|..
gi 1026594095 362 assdgTVKIWDT-KTTSCLHTV 382
Cdd:PTZ00421  238 -----QIMLWDTrKMASPYSTV 254
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 214-237 3.06e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.37  E-value: 3.06e-03
                           10        20
                   ....*....|....*....|....
gi 1026594095  214 CAVFSPNGQYIATGTVDGFIEIWN 237
Cdd:smart00320  17 SVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
214-237 7.32e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.24  E-value: 7.32e-03
                          10        20
                  ....*....|....*....|....
gi 1026594095 214 CAVFSPNGQYIATGTVDGFIEIWN 237
Cdd:pfam00400  16 SLAFSPDGKLLASGSDDGTVKVWD 39
 
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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