NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|330252606|gb|AEC07700|]
View 

transducin family protein / WD-40 repeat family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
392-661 3.79e-18

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 87.27  E-value: 3.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 392 IARLTYSPSGDYILALAEDATHKLWTWSSsqnefckenvypkPRLHQPQSGKTmenEMATSVqkstsCFAVKGSYLFSTS 471
Cdd:COG2319  123 VRSVAFSPDGKTLASGSADGTVRLWDLAT-------------GKLLRTLTGHS---GAVTSV-----AFSPDGKLLASGS 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 472 G-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFSRCFNVL 549
Cdd:COG2319  182 DdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPdGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLL 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 550 VSSDSDGKLCLWSTKSWVKLTSKNStrkfcnrsnleSTSLVTHIQFDPYQiELLVV--HDGWIGLYEVRTLdcRLQWIPD 627
Cdd:COG2319  262 ASGSADGTVRLWDLATGELLRTLTG-----------HSGGVNSVAFSPDG-KLLASgsDDGTVRLWDLATG--KLLRTLT 327

                        250       260       270
                 ....*....|....*....|....*....|....
gi 330252606 628 ASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKT 661
Cdd:COG2319  328 GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 191-221 1.70e-06

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: 44.73  E-value: 1.70e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 330252606   191 LKEDLICLILQFLYEAKYKNTLHKLEQETKV 221
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 7-37 6.52e-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: 40.50  E-value: 6.52e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 330252606     7 NRKNLVFLILQFFDEEGYEESLHLLEQDSGV 37
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 37-86 8.71e-03

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


:

Pssm-ID: 128914  Cd Length: 58  Bit Score: 35.24  E-value: 8.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 330252606    37 VFFDFSYLSNAILNGNWKDADDYLSAFTSPEANTFSrKMFFGLFKLKFSE 86
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNS-KLEFELRKQKFLE 49
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
392-661 3.79e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 87.27  E-value: 3.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 392 IARLTYSPSGDYILALAEDATHKLWTWSSsqnefckenvypkPRLHQPQSGKTmenEMATSVqkstsCFAVKGSYLFSTS 471
Cdd:COG2319  123 VRSVAFSPDGKTLASGSADGTVRLWDLAT-------------GKLLRTLTGHS---GAVTSV-----AFSPDGKLLASGS 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 472 G-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFSRCFNVL 549
Cdd:COG2319  182 DdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPdGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLL 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 550 VSSDSDGKLCLWSTKSWVKLTSKNStrkfcnrsnleSTSLVTHIQFDPYQiELLVV--HDGWIGLYEVRTLdcRLQWIPD 627
Cdd:COG2319  262 ASGSADGTVRLWDLATGELLRTLTG-----------HSGGVNSVAFSPDG-KLLASgsDDGTVRLWDLATG--KLLRTLT 327

                        250       260       270
                 ....*....|....*....|....*....|....
gi 330252606 628 ASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKT 661
Cdd:COG2319  328 GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 391-662 7.54e-16

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: 78.53  E-value: 7.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 391 KIARLTYSPSGDYILALAEDATHKLWTWSSSQNEFCKENvypkprlHQPqsgktmenematSVQKSTSCfaVKGSYLFST 470
Cdd:cd00200   11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG-------HTG------------PVRDVAAS--ADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 471 SG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFSRCFNV 548
Cdd:cd00200   70 SSdKTIRLWDLETGECVRTLTGHTSYVSSVAFSPdGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 549 LVSSDSDGKLCLWSTKSWVkltsknstrkfCNRSNLESTSLVTHIQFDPYQIELLV-VHDGWIGLYEVRTLDCrLQWIPd 627
Cdd:cd00200  150 VASSSQDGTIKLWDLRTGK-----------CVATLTGHTGEVNSVAFSPDGEKLLSsSSDGTIKLWDLSTGKC-LGTLR- 216

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 330252606 628 ASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKTF 662
Cdd:cd00200  217 GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG 251
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 191-221 1.70e-06

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: 44.73  E-value: 1.70e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 330252606   191 LKEDLICLILQFLYEAKYKNTLHKLEQETKV 221
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 523-562 5.08e-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: 5.08e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 330252606   523 SRKVKEKLEGHDQKITCLAFSRCFNVLVSSDSDGKLCLWS 562
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 505-558 6.50e-06

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: 44.96  E-value: 6.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 330252606  505 DLLAVGLDDGSIFIHCLSSRKV-KEKLEGHDQKITCLAFSRCFNVLVSSDSDGKL 558
Cdd:pfam12894   8 DLIALATEDGELLLHRLNWQRVwTLSPDKEDLEVTSLAWRPDGKLLAVGYSDGTV 62
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 7-37 6.52e-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: 40.50  E-value: 6.52e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 330252606     7 NRKNLVFLILQFFDEEGYEESLHLLEQDSGV 37
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
 9-37 3.37e-03

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: 35.45  E-value: 3.37e-03
                          10        20
                  ....*....|....*....|....*....
gi 330252606    9 KNLVFLILQFFDEEGYEESLHLLEQDSGV 37
Cdd:pfam17814   2 QDVVRLILQFLKENGLHRTLQALQTESGV 30
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 37-86 8.71e-03

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 35.24  E-value: 8.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 330252606    37 VFFDFSYLSNAILNGNWKDADDYLSAFTSPEANTFSrKMFFGLFKLKFSE 86
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNS-KLEFELRKQKFLE 49
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
392-661 3.79e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 87.27  E-value: 3.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 392 IARLTYSPSGDYILALAEDATHKLWTWSSsqnefckenvypkPRLHQPQSGKTmenEMATSVqkstsCFAVKGSYLFSTS 471
Cdd:COG2319  123 VRSVAFSPDGKTLASGSADGTVRLWDLAT-------------GKLLRTLTGHS---GAVTSV-----AFSPDGKLLASGS 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 472 G-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFSRCFNVL 549
Cdd:COG2319  182 DdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPdGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLL 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 550 VSSDSDGKLCLWSTKSWVKLTSKNStrkfcnrsnleSTSLVTHIQFDPYQiELLVV--HDGWIGLYEVRTLdcRLQWIPD 627
Cdd:COG2319  262 ASGSADGTVRLWDLATGELLRTLTG-----------HSGGVNSVAFSPDG-KLLASgsDDGTVRLWDLATG--KLLRTLT 327

                        250       260       270
                 ....*....|....*....|....*....|....
gi 330252606 628 ASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKT 661
Cdd:COG2319  328 GHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361
WD40 COG2319
WD40 repeat [General function prediction only];
392-661 3.38e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.50  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 392 IARLTYSPSGDYILALAEDATHKLWTWSSSQnefckenvyPKPRLHQPQSGktmenemATSVqkstsCFAVKGSYLFSTS 471
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLATGL---------LLRTLTGHTGA-------VRSV-----AFSPDGKTLASGS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 472 G-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFSRCFNVL 549
Cdd:COG2319  140 AdGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLL 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 550 VSSDSDGKLCLWSTKSWVKLTSKNStrkfcnrsnleSTSLVTHIQFDPYQiELLVV--HDGWIGLYEVRTLdcRLQWIPD 627
Cdd:COG2319  220 ASGSADGTVRLWDLATGKLLRTLTG-----------HSGSVRSVAFSPDG-RLLASgsADGTVRLWDLATG--ELLRTLT 285

                        250       260       270
                 ....*....|....*....|....*....|....
gi 330252606 628 ASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKT 661
Cdd:COG2319  286 GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLAT 319
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 391-662 7.54e-16

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: 78.53  E-value: 7.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 391 KIARLTYSPSGDYILALAEDATHKLWTWSSSQNEFCKENvypkprlHQPqsgktmenematSVQKSTSCfaVKGSYLFST 470
Cdd:cd00200   11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG-------HTG------------PVRDVAAS--ADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 471 SG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFSRCFNV 548
Cdd:cd00200   70 SSdKTIRLWDLETGECVRTLTGHTSYVSSVAFSPdGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTF 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 549 LVSSDSDGKLCLWSTKSWVkltsknstrkfCNRSNLESTSLVTHIQFDPYQIELLV-VHDGWIGLYEVRTLDCrLQWIPd 627
Cdd:cd00200  150 VASSSQDGTIKLWDLRTGK-----------CVATLTGHTGEVNSVAFSPDGEKLLSsSSDGTIKLWDLSTGKC-LGTLR- 216

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 330252606 628 ASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKTF 662
Cdd:cd00200  217 GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG 251
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 459-711 9.17e-16

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: 78.53  E-value: 9.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 459 CFAVKGSYLFSTSG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQK 536
Cdd:cd00200   16 AFSPDGKLLATGSGdGTIKVWDLETGELLRTLKGHTGPVRDVAASAdGTYLASGSSDKTIRLWDLETGECVRTLTGHTSY 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 537 ITCLAFSRCFNVLVSSDSDGKLCLWSTKSWVKLTSKNSTRKFcnrsnlestslVTHIQFDPYQieLLVV---HDGWIGLY 613
Cdd:cd00200   96 VSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDW-----------VNSVAFSPDG--TFVAsssQDGTIKLW 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 614 EVRTldCRLQWIPDASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKTFMTLCQinLTSFTQLSTSnislevyptvVAAH 693
Cdd:cd00200  163 DLRT--GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT--LRGHENGVNS----------VAFS 228

                        250
                 ....*....|....*...
gi 330252606 694 PSHpNQISAGLSNGKVIV 711
Cdd:cd00200  229 PDG-YLLASGSEDGTIRV 245
WD40 COG2319
WD40 repeat [General function prediction only];
389-661 5.04e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 74.56  E-value: 5.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 389 EEKIARLTYSPSGDYILALAEDATHKLWTWSSSQnefckenvypkpRLHQPQSGktmeNEMATSVqkstsCFAVKGSYLF 468
Cdd:COG2319  162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGK------------LLRTLTGH----TGAVRSV-----AFSPDGKLLA 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 469 STSG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFSRCF 546
Cdd:COG2319  221 SGSAdGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPdGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDG 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 547 NVLVSSDSDGKLCLWSTKSWVKLTSKNStrkfcnrsnleSTSLVTHIQFDPYQiELLVV--HDGWIGLYEVRTLDCrLQW 624
Cdd:COG2319  301 KLLASGSDDGTVRLWDLATGKLLRTLTG-----------HTGAVRSVAFSPDG-KTLASgsDDGTVRLWDLATGEL-LRT 367

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 330252606 625 IPDASDPaITSATYSSDGEIIYVGFRCGSIKIVDSKT 661
Cdd:COG2319  368 LTGHTGA-VTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 395-569 1.91e-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: 65.43  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 395 LTYSPSGDYILALAEDATHKLWTWSSSQNEFCkenvypkprlhqpqsgktmenemATSVQKSTSCFAVKGSYLFSTSG-- 472
Cdd:cd00200   99 VAFSPDGRILSSSSRDKTIKVWDVETGKCLTT-----------------------LRGHTDWVNSVAFSPDGTFVASSsq 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 473 -GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFSRCFNVLV 550
Cdd:cd00200  156 dGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPdGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLA 235

                        170
                 ....*....|....*....
gi 330252606 551 SSDSDGKLCLWSTKSWVKL 569
Cdd:cd00200  236 SGSEDGTIRVWDLRTGECV 254
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 395-562 1.96e-08

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 56.19  E-value: 1.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 395 LTYSPSGDYILALAEDATHKLWtwsssqnefckenvypkprlhQPQSGKTMENEMATSVQKSTSCFAVKGSYLFSTSG-G 473
Cdd:cd00200  141 VAFSPDGTFVASSSQDGTIKLW---------------------DLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSdG 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 474 KIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFSRCFNVLVSS 552
Cdd:cd00200  200 TIKLWDLSTGKCLGTLRGHENGVNSVAFSPdGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASG 279

                        170
                 ....*....|
gi 330252606 553 DSDGKLCLWS 562
Cdd:cd00200  280 SADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 530-711 2.58e-07

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 53.11  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 530 LEGHDQKITCLAFSRCFNVLVSSDSDGKLCLWSTKSWVKLtsknstrkfcnRSNLESTSLVTHIQFDPYQIELLVVH-DG 608
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL-----------RTLKGHTGPVRDVAASADGTYLASGSsDK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 609 WIGLYEVRTLDCRLQWIPDASDpaITSATYSSDGEIIYVGFRCGSIKIVDSKTFMtlCQINLTSFTQlstsnislevypT 688
Cdd:cd00200   74 TIRLWDLETGECVRTLTGHTSY--VSSVAFSPDGRILSSSSRDKTIKVWDVETGK--CLTTLRGHTD------------W 137

                        170       180
                 ....*....|....*....|....
gi 330252606 689 VVAAHPSHPNQ-ISAGLSNGKVIV 711
Cdd:cd00200  138 VNSVAFSPDGTfVASSSQDGTIKL 161
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 191-221 1.70e-06

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: 44.73  E-value: 1.70e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 330252606   191 LKEDLICLILQFLYEAKYKNTLHKLEQETKV 221
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 523-562 5.08e-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: 5.08e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 330252606   523 SRKVKEKLEGHDQKITCLAFSRCFNVLVSSDSDGKLCLWS 562
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 505-558 6.50e-06

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: 44.96  E-value: 6.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 330252606  505 DLLAVGLDDGSIFIHCLSSRKV-KEKLEGHDQKITCLAFSRCFNVLVSSDSDGKL 558
Cdd:pfam12894   8 DLIALATEDGELLLHRLNWQRVwTLSPDKEDLEVTSLAWRPDGKLLAVGYSDGTV 62
WD40 COG2319
WD40 repeat [General function prediction only];
499-661 5.15e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.44  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 499 FIFIPGDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFSRCFNVLVSSDSDGKLCLWSTKSwvkltsknstrKF 578
Cdd:COG2319   43 AASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLAT-----------GL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330252606 579 CNRSNLESTSLVTHIQFDPyQIELLVV--HDGWIGLYEVRTLDCrLQWIPDASDpAITSATYSSDGEIIYVGFRCGSIKI 656
Cdd:COG2319  112 LLRTLTGHTGAVRSVAFSP-DGKTLASgsADGTVRLWDLATGKL-LRTLTGHSG-AVTSVAFSPDGKLLASGSDDGTVRL 188


                 ....*
gi 330252606 657 VDSKT 661
Cdd:COG2319  189 WDLAT 193
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 7-37 6.52e-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: 40.50  E-value: 6.52e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 330252606     7 NRKNLVFLILQFFDEEGYEESLHLLEQDSGV 37
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
WD40 pfam00400
WD domain, G-beta repeat;
524-562 7.31e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.41  E-value: 7.31e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 330252606  524 RKVKEKLEGHDQKITCLAFSRCFNVLVSSDSDGKLCLWS 562
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
LisH_TPL pfam17814
LisH-like dimerization domain; TOPLESS (TPL) proteins have a highly conserved N-terminal ...
 9-37 3.37e-03

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: 35.45  E-value: 3.37e-03
                          10        20
                  ....*....|....*....|....*....
gi 330252606    9 KNLVFLILQFFDEEGYEESLHLLEQDSGV 37
Cdd:pfam17814   2 QDVVRLILQFLKENGLHRTLQALQTESGV 30
CTLH smart00668
C-terminal to LisH motif; Alpha-helical motif of unknown function.
 37-86 8.71e-03

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


Pssm-ID: 128914  Cd Length: 58  Bit Score: 35.24  E-value: 8.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 330252606    37 VFFDFSYLSNAILNGNWKDADDYLSAFTSPEANTFSrKMFFGLFKLKFSE 86
Cdd:smart00668   1 EFDERKRIRELILKGDWDEALEWLSSLKPPLLERNS-KLEFELRKQKFLE 49
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH