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Conserved domains on  [gi|1063708643|ref|NP_001319563|]
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Coatomer, beta' subunit [Arabidopsis thaliana]

Protein Classification

coatomer subunit beta'( domain architecture ID 17648131)

coatomer subunit beta' is a component of the coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network

Gene Ontology:  GO:0006891|GO:0006886|GO:0005198|GO:0006888
PubMed:  10322433

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Coatomer_WDAD_beta-like cd22947
Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', ...
 304-779 0e+00

Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', also called beta'-coat protein; beta'-COP; p102, is a component of the coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunit. It is a heptameric complex that can polymerize into a cage to deform the membrane into a bud. This model corresponds to the WD-associated (WDAD) region found in coatomer subunits beta and beta' and is composed of a beta-propeller and an alpha-solenoid. The WD40 domain is 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. It 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 the GH and WD lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet. 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. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands allowing them to bind either stably or reversibly.


:

Pssm-ID: 438572  Cd Length: 475  Bit Score: 845.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 304 PVASMDSSGKIIWAKHNEIQTANIKSIGAGyEATDGERLPLSVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALA 383
Cdd:cd22947     1 PAVSMDSSGKIIWAKHNEIQTANLKALDEE-EDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 384 WRNRSFGSGLEFVWSSEGEC-AVRESSSKIKIFsKNFQERKSIRPTFSAEKIFGGTLLAMCSNDFICFYDWAECRLIQQI 462
Cdd:cd22947    80 WRNKAFGSALEFVWSSDSNYyAVRESSSSVKIF-KNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 463 DVTVKNLYWAESGDLVAIASDTSFYILKYNRELVSSHFDSGRPTDEEGVEDAFEVLHENDERVRTGIWVGDCFIYNNSSW 542
Cdd:cd22947   159 DVEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSAN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 543 KLNYCVGGEVTTMYHLDRPMYLLGYIANQSRVYLVDKEFNVIGYTLLLSLIEYKTLVMRGDLDRANQILPTIPKEQHNNV 622
Cdd:cd22947   239 RLNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 623 AHFLESRGMIEDALEIATDPDYKFDLAIQLGRLEIAKEIAEEVQSESKWKQLGELAMSSGKLQLAEDCMKYAMDLSGLLL 702
Cdd:cd22947   319 ARFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLL 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063708643 703 LYSSLGDAEGVSKLACLAKEQGKNNVAFLCLFTLGRLEDCLQLLVESNRIPEAALMARSYLPSKVSEIVALWREDLS 779
Cdd:cd22947   399 LYSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 17-297 4.51e-67

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: 225.68  E-value: 4.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  17 RVKSVDLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNYNTMDKVKVFE 96
Cdd:cd00200    11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  97 AHSDYIRCVAVHPTLPYVLSSSDDMLIKLWDWENGwACTQIFEGHSHYVMQVVFNPkdTNTF-ASASLDRTIKIWNLGSP 175
Cdd:cd00200    91 GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 176 DPNFTLDAHQKGVNCVDYFTGGDKpyLITGSDDHTAKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRI 255
Cdd:cd00200   168 KCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1063708643 256 WHATTYRLENTLNYGLERVWAIGYIKSSRRVVIGYDEGTIMV 297
Cdd:cd00200   246 WDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
 
Name Accession Description Interval E-value
Coatomer_WDAD_beta-like cd22947
Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', ...
 304-779 0e+00

Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', also called beta'-coat protein; beta'-COP; p102, is a component of the coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunit. It is a heptameric complex that can polymerize into a cage to deform the membrane into a bud. This model corresponds to the WD-associated (WDAD) region found in coatomer subunits beta and beta' and is composed of a beta-propeller and an alpha-solenoid. The WD40 domain is 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. It 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 the GH and WD lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet. 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. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands allowing them to bind either stably or reversibly.


Pssm-ID: 438572  Cd Length: 475  Bit Score: 845.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 304 PVASMDSSGKIIWAKHNEIQTANIKSIGAGyEATDGERLPLSVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALA 383
Cdd:cd22947     1 PAVSMDSSGKIIWAKHNEIQTANLKALDEE-EDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 384 WRNRSFGSGLEFVWSSEGEC-AVRESSSKIKIFsKNFQERKSIRPTFSAEKIFGGTLLAMCSNDFICFYDWAECRLIQQI 462
Cdd:cd22947    80 WRNKAFGSALEFVWSSDSNYyAVRESSSSVKIF-KNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 463 DVTVKNLYWAESGDLVAIASDTSFYILKYNRELVSSHFDSGRPTDEEGVEDAFEVLHENDERVRTGIWVGDCFIYNNSSW 542
Cdd:cd22947   159 DVEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSAN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 543 KLNYCVGGEVTTMYHLDRPMYLLGYIANQSRVYLVDKEFNVIGYTLLLSLIEYKTLVMRGDLDRANQILPTIPKEQHNNV 622
Cdd:cd22947   239 RLNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 623 AHFLESRGMIEDALEIATDPDYKFDLAIQLGRLEIAKEIAEEVQSESKWKQLGELAMSSGKLQLAEDCMKYAMDLSGLLL 702
Cdd:cd22947   319 ARFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLL 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063708643 703 LYSSLGDAEGVSKLACLAKEQGKNNVAFLCLFTLGRLEDCLQLLVESNRIPEAALMARSYLPSKVSEIVALWREDLS 779
Cdd:cd22947   399 LYSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 319-764 0e+00

Coatomer WD associated region; This region is composed of WD40 repeats.


Pssm-ID: 427679  Cd Length: 439  Bit Score: 537.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 319 HNEIQTANIKSIgagyEATDGERLPLSVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALAWRNRSFGSGLEFVWS 398
Cdd:pfam04053   1 ENEVRSYNIKGI----ENKDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 399 SEGECAVRESSSKIKIFsKNFQER--KSIRPTFSAEKIFG---GTLLAMCSNDFICFYDWAECRLIQQIDVT-VKNLYWA 472
Cdd:pfam04053  77 SRNRFAVLEKSGTVKIF-KNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVSpVKYVIWS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 473 ESGDLVAIASDTSFYILKYNRELVsshfdsgrptdEEGVEDAFEVLHENDERVRTGIWVGDCFIYNNSSwKLNYCVGGEV 552
Cdd:pfam04053 156 DDGELVALLSKDTVYILNYNLEAV-----------EDGVEDAFEVLHEISERVKSGAWDGDVFIYTTSN-HLKYLVNGDS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 553 TTMYHLDRPMYLLGYIANQSRVYLVDKEFNVIGYTLLLSLIEYKTLVMRGDLD------RANQILPtiPKEQHNNVAHFL 626
Cdd:pfam04053 224 GIIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEevlriiRASNLLP--PKDEGQKIIRYL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 627 ESRGMIEDALEIATDPDYKFDLAIQLGRLEIAKEIAEEVQSESKWKQLGELAMSSGKLQLAEDCMKYAMDLSGLLLLYSS 706
Cdd:pfam04053 302 EKKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLS 381

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063708643 707 LGDAEGVSKLACLAKEQGKNNVAFLCLFTLGRLEDCLQLLVESNRIPEAALMARSYLP 764
Cdd:pfam04053 382 TGNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 17-297 4.51e-67

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: 225.68  E-value: 4.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  17 RVKSVDLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNYNTMDKVKVFE 96
Cdd:cd00200    11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  97 AHSDYIRCVAVHPTLPYVLSSSDDMLIKLWDWENGwACTQIFEGHSHYVMQVVFNPkdTNTF-ASASLDRTIKIWNLGSP 175
Cdd:cd00200    91 GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 176 DPNFTLDAHQKGVNCVDYFTGGDKpyLITGSDDHTAKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRI 255
Cdd:cd00200   168 KCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1063708643 256 WHATTYRLENTLNYGLERVWAIGYIKSSRRVVIGYDEGTIMV 297
Cdd:cd00200   246 WDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
9-297 5.69e-63

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 218.63  E-value: 5.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643   9 RKFAQRSERVKSVDLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNYNT 88
Cdd:COG2319   114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  89 MDKVKVFEAHSDYIRCVAVHPTLPYVLSSSDDMLIKLWDWENGwACTQIFEGHSHYVMQVVFNPkDTNTFASASLDRTIK 168
Cdd:COG2319   194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVR 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 169 IWNLGSPDPNFTLDAHQKGVNCVDyFTGGDKpYLITGSDDHTAKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGS 248
Cdd:COG2319   272 LWDLATGELLRTLTGHSGGVNSVA-FSPDGK-LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGS 349

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1063708643 249 EDGTVRIWHATTYRLENTLNYGLERVWAIGYIKSSRRVVIGYDEGTIMV 297
Cdd:COG2319   350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 218-257 3.71e-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: 58.48  E-value: 3.71e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1063708643  218 TKSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRIWH 257
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
219-256 7.56e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 54.66  E-value: 7.56e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1063708643 219 KSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRIW 256
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00421 PTZ00421
coronin; Provisional
 137-255 1.17e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 45.65  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 137 IFEGHSHYVMQVVFNPKDTNTFASASLDRTIKIWNL-------GSPDPNFTLDAHQKGVNCVDyFTGGDKPYLITGSDDH 209
Cdd:PTZ00421   70 ILLGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIpeegltqNISDPIVHLQGHTKKVGIVS-FHPSAMNVLASAGADM 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063708643 210 TAKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRI 255
Cdd:PTZ00421  149 VVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNI 194
 
Name Accession Description Interval E-value
Coatomer_WDAD_beta-like cd22947
Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', ...
 304-779 0e+00

Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', also called beta'-coat protein; beta'-COP; p102, is a component of the coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunit. It is a heptameric complex that can polymerize into a cage to deform the membrane into a bud. This model corresponds to the WD-associated (WDAD) region found in coatomer subunits beta and beta' and is composed of a beta-propeller and an alpha-solenoid. The WD40 domain is 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. It 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 the GH and WD lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet. 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. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands allowing them to bind either stably or reversibly.


Pssm-ID: 438572  Cd Length: 475  Bit Score: 845.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 304 PVASMDSSGKIIWAKHNEIQTANIKSIGAGyEATDGERLPLSVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALA 383
Cdd:cd22947     1 PAVSMDSSGKIIWAKHNEIQTANLKALDEE-EDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 384 WRNRSFGSGLEFVWSSEGEC-AVRESSSKIKIFsKNFQERKSIRPTFSAEKIFGGTLLAMCSNDFICFYDWAECRLIQQI 462
Cdd:cd22947    80 WRNKAFGSALEFVWSSDSNYyAVRESSSSVKIF-KNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 463 DVTVKNLYWAESGDLVAIASDTSFYILKYNRELVSSHFDSGRPTDEEGVEDAFEVLHENDERVRTGIWVGDCFIYNNSSW 542
Cdd:cd22947   159 DVEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSAN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 543 KLNYCVGGEVTTMYHLDRPMYLLGYIANQSRVYLVDKEFNVIGYTLLLSLIEYKTLVMRGDLDRANQILPTIPKEQHNNV 622
Cdd:cd22947   239 RLNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 623 AHFLESRGMIEDALEIATDPDYKFDLAIQLGRLEIAKEIAEEVQSESKWKQLGELAMSSGKLQLAEDCMKYAMDLSGLLL 702
Cdd:cd22947   319 ARFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLL 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063708643 703 LYSSLGDAEGVSKLACLAKEQGKNNVAFLCLFTLGRLEDCLQLLVESNRIPEAALMARSYLPSKVSEIVALWREDLS 779
Cdd:cd22947   399 LYSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 319-764 0e+00

Coatomer WD associated region; This region is composed of WD40 repeats.


Pssm-ID: 427679  Cd Length: 439  Bit Score: 537.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 319 HNEIQTANIKSIgagyEATDGERLPLSVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALAWRNRSFGSGLEFVWS 398
Cdd:pfam04053   1 ENEVRSYNIKGI----ENKDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 399 SEGECAVRESSSKIKIFsKNFQER--KSIRPTFSAEKIFG---GTLLAMCSNDFICFYDWAECRLIQQIDVT-VKNLYWA 472
Cdd:pfam04053  77 SRNRFAVLEKSGTVKIF-KNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVSpVKYVIWS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 473 ESGDLVAIASDTSFYILKYNRELVsshfdsgrptdEEGVEDAFEVLHENDERVRTGIWVGDCFIYNNSSwKLNYCVGGEV 552
Cdd:pfam04053 156 DDGELVALLSKDTVYILNYNLEAV-----------EDGVEDAFEVLHEISERVKSGAWDGDVFIYTTSN-HLKYLVNGDS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 553 TTMYHLDRPMYLLGYIANQSRVYLVDKEFNVIGYTLLLSLIEYKTLVMRGDLD------RANQILPtiPKEQHNNVAHFL 626
Cdd:pfam04053 224 GIIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEevlriiRASNLLP--PKDEGQKIIRYL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 627 ESRGMIEDALEIATDPDYKFDLAIQLGRLEIAKEIAEEVQSESKWKQLGELAMSSGKLQLAEDCMKYAMDLSGLLLLYSS 706
Cdd:pfam04053 302 EKKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLS 381

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063708643 707 LGDAEGVSKLACLAKEQGKNNVAFLCLFTLGRLEDCLQLLVESNRIPEAALMARSYLP 764
Cdd:pfam04053 382 TGNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
Coatomer_WDAD cd22938
Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds ...
 304-776 6.77e-163

Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunit. It is a heptameric complex that can polymerize into a cage to deform the membrane into a bud. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. This model corresponds to the WD-associated region (WDAD) found in coatomer subunits alpha, beta, and beta' and is composed of a beta-propeller and an alpha-solenoid. The WD40 domain is 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. It 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 the GH and WD lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet. 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. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands allowing them to bind either stably or reversibly.


Pssm-ID: 438571  Cd Length: 474  Bit Score: 484.50  E-value: 6.77e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 304 PVASMDSSGKIIWAKHNEiQTANIKSIGAGyEATDGERLPLSVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALA 383
Cdd:cd22938     1 PAYSVDGNGKLHWVKHSE-QQADRFLRQLD-FNSDGEKLVLVMKLRGSSKFPPQNMSHNPNGRFVLVCGDGEYDIYTAPA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 384 WRNRSFGSGLEFVWSSEG-ECAVRESSSKIKIFsKNFQERKS--IRPTFSAEKIFGGTLLAMCSNDFICFYDWAECRLIQ 460
Cdd:cd22938    79 GRNKSFGSAQTFVWVADSrFYALDRMHSSLKIK-KNFKEITSkiVPNCDEIFYAGTGNLLGVDSVDSITFFDWQNKRLLR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 461 QIDVTVKNLYWAESGDLVAIASDTSFYILKYNRELVSSHFDSGRPTDEEGVEDAFEVLHENDERVRTGIWVGDCFIYNNS 540
Cdd:cd22938   158 RIKIKVKYVIWSDDGELVAILAKHSIVILNYLSEKVLAAQETHEGVTEDGIERAFDVLCEIHERVKSGAWVGDVFIYTTS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 541 SWKLNYCVGGEVTTMYHLDRPMYLLGYIANQSRVYLVDKEFNVIGYTLLLSLIEYKTLVMRGDLDRANQILPTIPKEQHN 620
Cdd:cd22938   238 SNRLNYAVGGGHGIIAHLDLPMYLLGYKGNDNNVYLLDRECRPRVYTIDPTVLEFQTALIRRKYDMADEVLPMVRNAKRT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 621 NVAHFLESRGMIEDALEIATDPDYKFDLAIQLGRLEIAKEIAEEVQSESKWKQLGELAMSSGKLQLAEDCMKYAMDLSGL 700
Cdd:cd22938   318 RVAHFLEKQGFKQQALVGSSDIAYLFELALPEGALKIAYQLAHFVKDEKKWFSLALECGSKCNFELALEAAKAANDWEKL 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063708643 701 LLLYSSLGDAEGVSKLACLAKEQGKNNVAFLCLFTLGRLEDCLQLLVESNRIPEAALMARSYLPSKVSEIVALWRE 776
Cdd:cd22938   398 GLLALLQGNHQIVEMLAQRAENFGKNNKAFFLYLITGKLRKMMKLLIIRKRDMEAAFLNATYLGDQVSERVRIWKE 473
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 17-297 4.51e-67

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: 225.68  E-value: 4.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  17 RVKSVDLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNYNTMDKVKVFE 96
Cdd:cd00200    11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  97 AHSDYIRCVAVHPTLPYVLSSSDDMLIKLWDWENGwACTQIFEGHSHYVMQVVFNPkdTNTF-ASASLDRTIKIWNLGSP 175
Cdd:cd00200    91 GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 176 DPNFTLDAHQKGVNCVDYFTGGDKpyLITGSDDHTAKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRI 255
Cdd:cd00200   168 KCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1063708643 256 WHATTYRLENTLNYGLERVWAIGYIKSSRRVVIGYDEGTIMV 297
Cdd:cd00200   246 WDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
9-297 5.69e-63

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 218.63  E-value: 5.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643   9 RKFAQRSERVKSVDLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNYNT 88
Cdd:COG2319   114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  89 MDKVKVFEAHSDYIRCVAVHPTLPYVLSSSDDMLIKLWDWENGwACTQIFEGHSHYVMQVVFNPkDTNTFASASLDRTIK 168
Cdd:COG2319   194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVR 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 169 IWNLGSPDPNFTLDAHQKGVNCVDyFTGGDKpYLITGSDDHTAKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGS 248
Cdd:COG2319   272 LWDLATGELLRTLTGHSGGVNSVA-FSPDGK-LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGS 349

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1063708643 249 EDGTVRIWHATTYRLENTLNYGLERVWAIGYIKSSRRVVIGYDEGTIMV 297
Cdd:COG2319   350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
WD40 COG2319
WD40 repeat [General function prediction only];
9-297 1.19e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 209.38  E-value: 1.19e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643   9 RKFAQRSERVKSVDLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNYNT 88
Cdd:COG2319    72 ATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  89 MDKVKVFEAHSDYIRCVAVHPTLPYVLSSSDDMLIKLWDWENGwACTQIFEGHSHYVMQVVFNPkDTNTFASASLDRTIK 168
Cdd:COG2319   152 GKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVR 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 169 IWNLGSPDPNFTLDAHQKGVNCVDYFTGGDkpYLITGSDDHTAKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGS 248
Cdd:COG2319   230 LWDLATGKLLRTLTGHSGSVRSVAFSPDGR--LLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGS 307

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1063708643 249 EDGTVRIWHATTYRLENTLNYGLERVWAIGYIKSSRRVVIGYDEGTIMV 297
Cdd:COG2319   308 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
WD40 COG2319
WD40 repeat [General function prediction only];
15-260 6.95e-58

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 204.37  E-value: 6.95e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  15 SERVKSVDLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNYNTMDKVKV 94
Cdd:COG2319   162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  95 FEAHSDYIRCVAVHPTLPYVLSSSDDMLIKLWDWENGwACTQIFEGHSHYVMQVVFNPkDTNTFASASLDRTIKIWNLGS 174
Cdd:COG2319   242 LTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG-ELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLAT 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 175 PDPNFTLDAHQKGVNCVDYFTGGDkpYLITGSDDHTAKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVR 254
Cdd:COG2319   320 GKLLRTLTGHTGAVRSVAFSPDGK--TLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVR 397


                  ....*.
gi 1063708643 255 IWHATT 260
Cdd:COG2319   398 LWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
11-297 1.40e-55

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 197.83  E-value: 1.40e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  11 FAQRSERVKSVDLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNYNTMD 90
Cdd:COG2319    32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  91 KVKVFEAHSDYIRCVAVHPTLPYVLSSSDDMLIKLWDWENGwACTQIFEGHSHYVMQVVFNPkDTNTFASASLDRTIKIW 170
Cdd:COG2319   112 LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATG-KLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGTVRLW 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 171 NLGSPDPNFTLDAHQKGVNCVDYFTGGDkpYLITGSDDHTAKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGSED 250
Cdd:COG2319   190 DLATGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSAD 267

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1063708643 251 GTVRIWHATTYRLENTLNYGLERVWAIGYIKSSRRVVIGYDEGTIMV 297
Cdd:COG2319   268 GTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRL 314
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 9-215 2.58e-49

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: 176.37  E-value: 2.58e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643   9 RKFAQRSERVKSVDLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNYNT 88
Cdd:cd00200    87 RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  89 MDKVKVFEAHSDYIRCVAVHPTLPYVLSSSDDMLIKLWDWENGwACTQIFEGHSHYVMQVVFNPkDTNTFASASLDRTIK 168
Cdd:cd00200   167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG-KCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIR 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1063708643 169 IWNLGSPDPNFTLDAHQKGVNCVDYFTggDKPYLITGSDDHTAKVWD 215
Cdd:cd00200   245 VWDLRTGECVQTLSGHTNSVTSLAWSP--DGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
22-297 2.91e-47

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 173.94  E-value: 2.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  22 DLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNYNTMDKVKVFEAHSDY 101
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 102 IRCVAVHPTLPYVLSSSDDMLIKLWDWENGwACTQIFEGHSHYVMQVVFNPkDTNTFASASLDRTIKIWNLGSPDPNFTL 181
Cdd:COG2319    81 VLSVAFSPDGRLLASASADGTVRLWDLATG-LLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLATGKLLRTL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 182 DAHQKGVNCVDYFTGGDkpYLITGSDDHTAKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRIWHATTY 261
Cdd:COG2319   159 TGHSGAVTSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG 236

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1063708643 262 RLENTLNYGLERVWAIGYIKSSRRVVIGYDEGTIMV 297
Cdd:COG2319   237 KLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRL 272
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 92-297 4.44e-46

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: 167.13  E-value: 4.44e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  92 VKVFEAHSDYIRCVAVHPTLPYVLSSSDDMLIKLWDWENG------------------------------------W--- 132
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGellrtlkghtgpvrdvaasadgtylasgssdktirlWdle 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 133 --ACTQIFEGHSHYVMQVVFNPKDTnTFASASLDRTIKIWNLGSPDPNFTLDAHQKGVNCVDYftGGDKPYLITGSDDHT 210
Cdd:cd00200    82 tgECVRTLTGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAF--SPDGTFVASSSQDGT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 211 AKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRIWHATTYRLENTLNYGLERVWAIGYIKSSRRVVIGY 290
Cdd:cd00200   159 IKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGS 238


                  ....*..
gi 1063708643 291 DEGTIMV 297
Cdd:cd00200   239 EDGTIRV 245
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 134-297 1.38e-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: 145.56  E-value: 1.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 134 CTQIFEGHSHYVMQVVFNPkDTNTFASASLDRTIKIWNLGSPDPNFTLDAHQKGVNCVDYFtgGDKPYLITGSDDHTAKV 213
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAS--ADGTYLASGSSDKTIRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 214 WDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRIWHATTYRLENTLNYGLERVWAIGYIKSSRRVVIGYDEG 293
Cdd:cd00200    78 WDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157


                  ....
gi 1063708643 294 TIMV 297
Cdd:cd00200   158 TIKL 161
Coatomer_WDAD_alpha cd22948
Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called ...
 356-762 8.92e-29

Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called alpha-coat protein; Alpha-COP; HEPCOP, is a component of the coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunit. It is a heptameric complex that can polymerize into a cage to deform the membrane into a bud. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. This model corresponds to the WD-associated region (WDAD) found in coatomer subunit alpha and is composed of a beta-propeller and an alpha-solenoid. The WD40 domain is 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. It 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 the GH and WD lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet. 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. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands allowing them to bind either stably or reversibly.


Pssm-ID: 438573  Cd Length: 452  Bit Score: 120.70  E-value: 8.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 356 PQSLKHNPNGRFVVVCGDGE------YIIYTALAWRN----RSFGSGLEFVWSSEGECAVRESSSKIKIfsKNFQ--ERK 423
Cdd:cd22948    46 PRSLSYNPAENAVLVTSDADggsyelYTLPKDSSGAPekpeSKRGSGLSAVFVARNRFAVLDKSGTILI--KNLEneVTK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 424 SIRPTFSAEKIFGGT----LLAmcSNDFICFYDWAECRLIQQIDVT-VKNLYWAESGDLVAIASDTSFYILKYNRELVSS 498
Cdd:cd22948   124 KIKPPPNVDKIFYAGtgrvLLR--SEDKVILFDVQQKRVLAEVKVPkVKYVVWSKDMSHVALLSKHSITIATKKLEQLCS 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 499 hfdsgrptdeegvedafevLHENDeRVRTGIWVGD-CFIYNNSSwKLNYC-VGGEVTTMYHLDRPMYLLGYIANQsrVYL 576
Cdd:cd22948   202 -------------------VHETI-RIKSGAWDESgVLIYTTLN-HIKYLlPNGDSGIIRTLDSPIYLTRVKGNT--VYC 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 577 VDKEFNVigYTLLLSLIEY--KTLVMRGDLDRANQILptipkeQHNN-----VAHFLESRGMIEDALEIATDPDYKFDLA 649
Cdd:cd22948   259 LDREGKV--RVLEIDPTEYlfKLALINKNYDEVLRII------RSSKlvgqsIIAYLQKKGYPEIALHFVKDPKTRFNLA 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 650 IQLGRLEIAKEIAEEVQSESKWKQLGELAMSSGKLQLAEDCMK-----------YAMdlsgllllyssLGDAEGVSKLAC 718
Cdd:cd22948   331 LECGNLEVALEAAKELDDPECWERLAEEALRQGNHQIVEMAYQktknfdklsflYLI-----------TGNLEKLRKMLK 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1063708643 719 LAKEQGKNNVAFLCLFTLGRLEDCLQLLVESNRIPEAALMARSY 762
Cdd:cd22948   400 IAEKRGDVMSRFQNALYLGDVEERVKILKEAGQLPLAYLTAKTH 443
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 8-127 3.59e-20

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: 92.01  E-value: 3.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643   8 KRKFAQRSERVKSVDLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNYN 87
Cdd:cd00200   170 VATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLR 249

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1063708643  88 TMDKVKVFEAHSDYIRCVAVHPTLPYVLSSSDDMLIKLWD 127
Cdd:cd00200   250 TGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
7-130 3.02e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.88  E-value: 3.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643   7 IKRKFAQRSERVKSVDLHPTEPWILASLYSGTVCIWNYQTQTITKSFEVTELPVRSAKFIPRKQWVVAGADDMYIRVYNY 86
Cdd:COG2319   280 LLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063708643  87 NTMDKVKVFEAHSDYIRCVAVHPTLPYVLSSSDDMLIKLWDWEN 130
Cdd:COG2319   360 ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 218-257 3.71e-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: 58.48  E-value: 3.71e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1063708643  218 TKSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRIWH 257
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
219-256 7.56e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 54.66  E-value: 7.56e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1063708643 219 KSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRIW 256
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 88-127 6.16e-08

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: 49.62  E-value: 6.16e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1063708643   88 TMDKVKVFEAHSDYIRCVAVHPTLPYVLSSSDDMLIKLWD 127
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
92-127 2.26e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.73  E-value: 2.26e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1063708643  92 VKVFEAHSDYIRCVAVHPTLPYVLSSSDDMLIKLWD 127
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 132-171 2.84e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 47.69  E-value: 2.84e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1063708643  132 WACTQIFEGHSHYVMQVVFNPkDTNTFASASLDRTIKIWN 171
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
132-171 1.09e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 1.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1063708643 132 WACTQIFEGHSHYVMQVVFNPkDTNTFASASLDRTIKIWN 171
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 179-215 6.12e-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: 6.12e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1063708643  179 FTLDAHQKGVNCVDYFtgGDKPYLITGSDDHTAKVWD 215
Cdd:smart00320   6 KTLKGHTGPVTSVAFS--PDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
177-215 7.70e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.49  E-value: 7.70e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1063708643 177 PNFTLDAHQKGVNCVDYFTggDKPYLITGSDDHTAKVWD 215
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSP--DGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 137-255 1.17e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 45.65  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 137 IFEGHSHYVMQVVFNPKDTNTFASASLDRTIKIWNL-------GSPDPNFTLDAHQKGVNCVDyFTGGDKPYLITGSDDH 209
Cdd:PTZ00421   70 ILLGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIpeegltqNISDPIVHLQGHTKKVGIVS-FHPSAMNVLASAGADM 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063708643 210 TAKVWDYQTKSCVQTLDGHTHNVSAVCFHPELPIIITGSEDGTVRI 255
Cdd:PTZ00421  149 VVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNI 194
PTZ00421 PTZ00421
coronin; Provisional
 87-269 1.63e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 45.27  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643  87 NTMDKVKVFEAHSDYIRCVAVHPTLPYVLSSSD-DMLIKLWDWENGWACTQIfEGHSHYVMQVVFNpKDTNTFASASLDR 165
Cdd:PTZ00421  113 NISDPIVHLQGHTKKVGIVSFHPSAMNVLASAGaDMVVNVWDVERGKAVEVI-KCHSDQITSLEWN-LDGSLLCTTSKDK 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 166 TIKIWNLGSPDPNFTLDAHQ--KGVNCVdyfTGGDKPYLIT----GSDDHTAKVWDYQT-KSCVQTLD-GHTHNVSAVCF 237
Cdd:PTZ00421  191 KLNIIDPRDGTIVSSVEAHAsaKSQRCL---WAKRKDLIITlgcsKSQQRQIMLWDTRKmASPYSTVDlDQSSALFIPFF 267

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1063708643 238 HPELPIIITGSE-DGTVRIWHATTYRLENTLNY 269
Cdd:PTZ00421  268 DEDTNLLYIGSKgEGNIRCFELMNERLTFCSSY 300
PTZ00420 PTZ00420
coronin; Provisional
 138-215 3.49e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 41.09  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063708643 138 FEGHSHYVMQVVFNPKDTNTFASASLDRTIKIWNLGS--------PDPNFTLDAHQKGVNCVDYftgGDKPYLITGSD-- 207
Cdd:PTZ00420   70 LKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHndesvkeiKDPQCILKGHKKKISIIDW---NPMNYYIMCSSgf 146


                  ....*...
gi 1063708643 208 DHTAKVWD 215
Cdd:PTZ00420  147 DSFVNIWD 154
 
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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