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Conserved domains on  [gi|1063704814|ref|NP_001325217|]
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transducin family protein / WD-40 repeat family protein [Arabidopsis thaliana]

Protein Classification

LisH and WD40 domain-containing protein( domain architecture ID 12217999)

LisH and WD40 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
392-668 2.63e-17

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 84.58  E-value: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 392 IARLTYSPSGDYILALAEDATHKLWTWSSsqnefckytpkilkenvypkPRLHQPQSGKTmenEMATSVqkstsCFAVKG 471
Cdd:COG2319   123 VRSVAFSPDGKTLASGSADGTVRLWDLAT--------------------GKLLRTLTGHS---GAVTSV-----AFSPDG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 472 SYLFSTSG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAF 549
Cdd:COG2319   175 KLLASGSDdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPdGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAF 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 550 SRCFNVLVSSDSDGKLCLWSTKSWVKLTSKNStrkfcnrsnleSTSLVTHIQFDPYQiELLVV--HDGWIGLYEVRTLdc 627
Cdd:COG2319   255 SPDGRLLASGSADGTVRLWDLATGELLRTLTG-----------HSGGVNSVAFSPDG-KLLASgsDDGTVRLWDLATG-- 320

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1063704814 628 RLQWIPDASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKT 668
Cdd:COG2319   321 KLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 191-221 2.38e-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: 44.35  E-value: 2.38e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1063704814  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 8.79e-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: 40.11  E-value: 8.79e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1063704814    7 NRKNLVFLILQFFDEEGYEESLHLLEQDSGV 37
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
392-668 2.63e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 84.58  E-value: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 392 IARLTYSPSGDYILALAEDATHKLWTWSSsqnefckytpkilkenvypkPRLHQPQSGKTmenEMATSVqkstsCFAVKG 471
Cdd:COG2319   123 VRSVAFSPDGKTLASGSADGTVRLWDLAT--------------------GKLLRTLTGHS---GAVTSV-----AFSPDG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 472 SYLFSTSG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAF 549
Cdd:COG2319   175 KLLASGSDdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPdGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAF 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 550 SRCFNVLVSSDSDGKLCLWSTKSWVKLTSKNStrkfcnrsnleSTSLVTHIQFDPYQiELLVV--HDGWIGLYEVRTLdc 627
Cdd:COG2319   255 SPDGRLLASGSADGTVRLWDLATGELLRTLTG-----------HSGGVNSVAFSPDG-KLLASgsDDGTVRLWDLATG-- 320

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1063704814 628 RLQWIPDASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKT 668
Cdd:COG2319   321 KLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 466-675 7.96e-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: 7.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 466 CFAVKGSYLFSTSG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQK 543
Cdd:cd00200    16 AFSPDGKLLATGSGdGTIKVWDLETGELLRTLKGHTGPVRDVAASAdGTYLASGSSDKTIRLWDLETGECVRTLTGHTSY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 544 ITCLAFSRCFNVLVSSDSDGKLCLWSTKSWVKLTSKNSTRKFcnrsnlestslVTHIQFDPYQieLLVV---HDGWIGLY 620
Cdd:cd00200    96 VSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDW-----------VNSVAFSPDG--TFVAsssQDGTIKLW 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063704814 621 EVRTldCRLQWIPDASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKTFMTLCQI 675
Cdd:cd00200   163 DLRT--GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTL 215
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 191-221 2.38e-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: 44.35  E-value: 2.38e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1063704814  191 LKEDLICLILQFLYEAKYKNTLHKLEQETKV 221
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 530-569 4.19e-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: 4.19e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1063704814  530 SRKVKEKLEGHDQKITCLAFSRCFNVLVSSDSDGKLCLWS 569
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 512-565 4.89e-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: 45.35  E-value: 4.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063704814 512 DLLAVGLDDGSIFIHCLSSRKV-KEKLEGHDQKITCLAFSRCFNVLVSSDSDGKL 565
Cdd:pfam12894   8 DLIALATEDGELLLHRLNWQRVwTLSPDKEDLEVTSLAWRPDGKLLAVGYSDGTV 62
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 7-37 8.79e-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: 40.11  E-value: 8.79e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1063704814    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 3.19e-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: 3.19e-03
                          10        20
                  ....*....|....*....|....*....
gi 1063704814   9 KNLVFLILQFFDEEGYEESLHLLEQDSGV 37
Cdd:pfam17814   2 QDVVRLILQFLKENGLHRTLQALQTESGV 30
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
392-668 2.63e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 84.58  E-value: 2.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 392 IARLTYSPSGDYILALAEDATHKLWTWSSsqnefckytpkilkenvypkPRLHQPQSGKTmenEMATSVqkstsCFAVKG 471
Cdd:COG2319   123 VRSVAFSPDGKTLASGSADGTVRLWDLAT--------------------GKLLRTLTGHS---GAVTSV-----AFSPDG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 472 SYLFSTSG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAF 549
Cdd:COG2319   175 KLLASGSDdGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPdGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAF 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 550 SRCFNVLVSSDSDGKLCLWSTKSWVKLTSKNStrkfcnrsnleSTSLVTHIQFDPYQiELLVV--HDGWIGLYEVRTLdc 627
Cdd:COG2319   255 SPDGRLLASGSADGTVRLWDLATGELLRTLTG-----------HSGGVNSVAFSPDG-KLLASgsDDGTVRLWDLATG-- 320

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1063704814 628 RLQWIPDASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKT 668
Cdd:COG2319   321 KLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLAT 361
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 466-675 7.96e-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: 7.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 466 CFAVKGSYLFSTSG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQK 543
Cdd:cd00200    16 AFSPDGKLLATGSGdGTIKVWDLETGELLRTLKGHTGPVRDVAASAdGTYLASGSSDKTIRLWDLETGECVRTLTGHTSY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 544 ITCLAFSRCFNVLVSSDSDGKLCLWSTKSWVKLTSKNSTRKFcnrsnlestslVTHIQFDPYQieLLVV---HDGWIGLY 620
Cdd:cd00200    96 VSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDW-----------VNSVAFSPDG--TFVAsssQDGTIKLW 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063704814 621 EVRTldCRLQWIPDASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKTFMTLCQI 675
Cdd:cd00200   163 DLRT--GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTL 215
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 391-669 9.86e-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: 78.15  E-value: 9.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 391 KIARLTYSPSGDYILALAEDATHKLWTWSSSQnefCKYTPKILKENVypkprlhqpqsgktmenematsVQKSTSCFavk 470
Cdd:cd00200    11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGE---LLRTLKGHTGPV----------------------RDVAASAD--- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 471 GSYLFSTSG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLA 548
Cdd:cd00200    63 GTYLASGSSdKTIRLWDLETGECVRTLTGHTSYVSSVAFSPdGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVA 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 549 FSRCFNVLVSSDSDGKLCLWSTKSWVkltsknstrkfCNRSNLESTSLVTHIQFDPYQIELLV-VHDGWIGLYEVRTLDC 627
Cdd:cd00200   143 FSPDGTFVASSSQDGTIKLWDLRTGK-----------CVATLTGHTGEVNSVAFSPDGEKLLSsSSDGTIKLWDLSTGKC 211

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1063704814 628 rLQWIPdASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKTF 669
Cdd:cd00200   212 -LGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG 251
WD40 COG2319
WD40 repeat [General function prediction only];
392-668 1.42e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.18  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 392 IARLTYSPSGDYILALAEDATHKLWTWSSSQnefCKYTPKILKENVypkprlhqpqsgktmenemaTSVqkstsCFAVKG 471
Cdd:COG2319    81 VLSVAFSPDGRLLASASADGTVRLWDLATGL---LLRTLTGHTGAV--------------------RSV-----AFSPDG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 472 SYLFSTSG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAF 549
Cdd:COG2319   133 KTLASGSAdGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPdGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAF 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 550 SRCFNVLVSSDSDGKLCLWSTKSWVKLTSKNStrkfcnrsnleSTSLVTHIQFDPYQiELLVV--HDGWIGLYEVRTLdc 627
Cdd:COG2319   213 SPDGKLLASGSADGTVRLWDLATGKLLRTLTG-----------HSGSVRSVAFSPDG-RLLASgsADGTVRLWDLATG-- 278

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1063704814 628 RLQWIPDASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKT 668
Cdd:COG2319   279 ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLAT 319
WD40 COG2319
WD40 repeat [General function prediction only];
389-668 1.41e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 73.02  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 389 EEKIARLTYSPSGDYILALAEDATHKLWTWSSSQnefckyTPKILKEnvypkprlHQpqsgktmenEMATSVqkstsCFA 468
Cdd:COG2319   162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGK------LLRTLTG--------HT---------GAVRSV-----AFS 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 469 VKGSYLFSTSG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITC 546
Cdd:COG2319   214 PDGKLLASGSAdGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPdGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNS 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 547 LAFSRCFNVLVSSDSDGKLCLWSTKSWVKLTSKNStrkfcnrsnleSTSLVTHIQFDPYQiELLVV--HDGWIGLYEVRT 624
Cdd:COG2319   294 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG-----------HTGAVRSVAFSPDG-KTLASgsDDGTVRLWDLAT 361

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1063704814 625 LDCrLQWIPDASDPaITSATYSSDGEIIYVGFRCGSIKIVDSKT 668
Cdd:COG2319   362 GEL-LRTLTGHTGA-VTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 395-576 3.50e-11

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 64.66  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 395 LTYSPSGDYILALAEDATHKLWTWSSSQnefCKYTpkilkenvypkprlhqpqsgktmenemATSVQKSTSCFAVKGSYL 474
Cdd:cd00200    99 VAFSPDGRILSSSSRDKTIKVWDVETGK---CLTT---------------------------LRGHTDWVNSVAFSPDGT 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 475 FSTSG---GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFS 550
Cdd:cd00200   149 FVASSsqdGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPdGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFS 228

                         170       180
                  ....*....|....*....|....*.
gi 1063704814 551 RCFNVLVSSDSDGKLCLWSTKSWVKL 576
Cdd:cd00200   229 PDGYLLASGSEDGTIRVWDLRTGECV 254
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 395-569 4.80e-09

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: 58.12  E-value: 4.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 395 LTYSPSGDYILALAEDATHKLWtwsSSQNEFCKYTPKILKENVYpkprlhqpqsgktmenematsvqksTSCFAVKGSYL 474
Cdd:cd00200   141 VAFSPDGTFVASSSQDGTIKLW---DLRTGKCVATLTGHTGEVN-------------------------SVAFSPDGEKL 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 475 FSTSG-GKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKEKLEGHDQKITCLAFSRC 552
Cdd:cd00200   193 LSSSSdGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPdGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPD 272

                         170
                  ....*....|....*..
gi 1063704814 553 FNVLVSSDSDGKLCLWS 569
Cdd:cd00200   273 GKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
457-668 1.76e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.23  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 457 ATSVQKSTSCFAVKGSYLFSTSGGKIAVFDLKNFEKVASFGSPTPMATYFIFIP-GDLLAVGLDDGSIFIHCLSSRKVKE 535
Cdd:COG2319    35 LAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPdGRLLASASADGTVRLWDLATGLLLR 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 536 KLEGHDQKITCLAFSRCFNVLVSSDSDGKLCLWSTKSWVKLTSKNstrkfcnrsnlESTSLVTHIQFDPyQIELLVV--H 613
Cdd:COG2319   115 TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT-----------GHSGAVTSVAFSP-DGKLLASgsD 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063704814 614 DGWIGLYEVRTLDCRLQWipDASDPAITSATYSSDGEIIYVGFRCGSIKIVDSKT 668
Cdd:COG2319   183 DGTVRLWDLATGKLLRTL--TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT 235
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 537-681 2.32e-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: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063704814 537 LEGHDQKITCLAFSRCFNVLVSSDSDGKLCLWSTKSWVKLtsknstrkfcnRSNLESTSLVTHIQFDPYQIELLVVH-DG 615
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL-----------RTLKGHTGPVRDVAASADGTYLASGSsDK 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063704814 616 WIGLYEVRTLDCRLQWIPDASDpaITSATYSSDGEIIYVGFRCGSIKIVDSKTFMtlCQINLTSFT 681
Cdd:cd00200    74 TIRLWDLETGECVRTLTGHTSY--VSSVAFSPDGRILSSSSRDKTIKVWDVETGK--CLTTLRGHT 135
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 191-221 2.38e-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: 44.35  E-value: 2.38e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1063704814  191 LKEDLICLILQFLYEAKYKNTLHKLEQETKV 221
Cdd:smart00667   2 SRSELNRLILEYLLRNGYEETAETLQKESGL 32
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 530-569 4.19e-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: 4.19e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1063704814  530 SRKVKEKLEGHDQKITCLAFSRCFNVLVSSDSDGKLCLWS 569
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 512-565 4.89e-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: 45.35  E-value: 4.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063704814 512 DLLAVGLDDGSIFIHCLSSRKV-KEKLEGHDQKITCLAFSRCFNVLVSSDSDGKL 565
Cdd:pfam12894   8 DLIALATEDGELLLHRLNWQRVwTLSPDKEDLEVTSLAWRPDGKLLAVGYSDGTV 62
WD40 pfam00400
WD domain, G-beta repeat;
531-569 5.68e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 40.79  E-value: 5.68e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1063704814 531 RKVKEKLEGHDQKITCLAFSRCFNVLVSSDSDGKLCLWS 569
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
LisH smart00667
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ...
 7-37 8.79e-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: 40.11  E-value: 8.79e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1063704814    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 3.19e-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: 3.19e-03
                          10        20
                  ....*....|....*....|....*....
gi 1063704814   9 KNLVFLILQFFDEEGYEESLHLLEQDSGV 37
Cdd:pfam17814   2 QDVVRLILQFLKENGLHRTLQALQTESGV 30
 
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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