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Conserved domains on  [gi|238479136|ref|NP_001154480|]
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coatomer subunit beta-2 [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', ...
 304-777 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: 850.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 304 PVASMDNSGKIIWAKHNEIHTVNIKSVGADEVTDGERLPLAVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALAW 383
Cdd:cd22947    1 PAVSMDSSGKIIWAKHNEIQTANLKALDEEEDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALAW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 384 RNRSFGSALEFVWSSDG-EHAVRESSTKIKIFsKNFQEKKTVRPTFSAEHIFGGTLLTMCSSDFICFYDWAECRLIRRID 462
Cdd:cd22947   81 RNKAFGSALEFVWSSDSnYYAVRESSSSVKIF-KNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRID 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 463 VTVKNLYWADSGDLVAIASDTSFYILKFNRDIVSSYFDGGKQIDEEGIEDAFELLNETNERVRTGLWVGDCFIYTNSSWR 542
Cdd:cd22947  160 VEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSANR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 543 LNYCVGGEVTTMYHLDRPMYLLGYLANQSRVYLIDKEFNVIGYTLLLSLIEYKTLVMRGDLEQANEVLPSIPKEHHNSVA 622
Cdd:cd22947  240 LNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKVA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 623 HFLESRGMTEDALEVATDPDYRFELAIQLGRLAVAKDIAVEAQNESKWKQLGELAMSSGKLDMAEECMRHAMDLSGLLLL 702
Cdd:cd22947  320 RFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLLL 399

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238479136 703 YSSLGDADGMMKLAALAKEQGKNNVAFLCLFMLGQVEDCLHLLVESNRIPEAALMARSYLPSKVSEIVALWRNDL 777
Cdd:cd22947  400 YSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDL 474
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 17-297 9.38e-65

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: 219.51  E-value: 9.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  17 RVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVYNYNTMDKIKVFE 96
Cdd:cd00200   11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  97 AHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGwLCTQIFEGHSHYVMQVTFNPkdTNTF-ASASLDRTIKIWNLGSP 175
Cdd:cd00200   91 GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTG 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 176 DPNFTLDAHLKGVNCVDYFTGGDKpyLITGSDDHTAKVWDYQTKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRI 255
Cdd:cd00200  168 KCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 238479136 256 WHATTYRLENTLNYGLERVWAIGHIKGSRRVVIGYDEGSIMV 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', ...
 304-777 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: 850.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 304 PVASMDNSGKIIWAKHNEIHTVNIKSVGADEVTDGERLPLAVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALAW 383
Cdd:cd22947    1 PAVSMDSSGKIIWAKHNEIQTANLKALDEEEDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALAW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 384 RNRSFGSALEFVWSSDG-EHAVRESSTKIKIFsKNFQEKKTVRPTFSAEHIFGGTLLTMCSSDFICFYDWAECRLIRRID 462
Cdd:cd22947   81 RNKAFGSALEFVWSSDSnYYAVRESSSSVKIF-KNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRID 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 463 VTVKNLYWADSGDLVAIASDTSFYILKFNRDIVSSYFDGGKQIDEEGIEDAFELLNETNERVRTGLWVGDCFIYTNSSWR 542
Cdd:cd22947  160 VEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSANR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 543 LNYCVGGEVTTMYHLDRPMYLLGYLANQSRVYLIDKEFNVIGYTLLLSLIEYKTLVMRGDLEQANEVLPSIPKEHHNSVA 622
Cdd:cd22947  240 LNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKVA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 623 HFLESRGMTEDALEVATDPDYRFELAIQLGRLAVAKDIAVEAQNESKWKQLGELAMSSGKLDMAEECMRHAMDLSGLLLL 702
Cdd:cd22947  320 RFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLLL 399

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238479136 703 YSSLGDADGMMKLAALAKEQGKNNVAFLCLFMLGQVEDCLHLLVESNRIPEAALMARSYLPSKVSEIVALWRNDL 777
Cdd:cd22947  400 YSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDL 474
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 319-763 0e+00

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 531.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  319 HNEIHTVNIKSVGAdevTDGERLPLAVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALAWRNRSFGSALEFVWSS 398
Cdd:pfam04053   1 ENEVRSYNIKGIEN---KDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  399 DGEHAVRESSTKIKIFsKNFQEK--KTVRPTFSAEHIFG---GTLLTMCSSDFICFYDWAECRLIRRIDVT-VKNLYWAD 472
Cdd:pfam04053  78 RNRFAVLEKSGTVKIF-KNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVSpVKYVIWSD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  473 SGDLVAIASDTSFYILKFNRDIVssyfdggkqidEEGIEDAFELLNETNERVRTGLWVGDCFIYTNSSwRLNYCVGGEVT 552
Cdd:pfam04053 157 DGELVALLSKDTVYILNYNLEAV-----------EDGVEDAFEVLHEISERVKSGAWDGDVFIYTTSN-HLKYLVNGDSG 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  553 TMYHLDRPMYLLGYLANQSRVYLIDKEFNVIGYTLLLSLIEYKTLVMRGDLEQ------ANEVLPsiPKEHHNSVAHFLE 626
Cdd:pfam04053 225 IIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEEvlriirASNLLP--PKDEGQKIIRYLE 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  627 SRGMTEDALEVATDPDYRFELAIQLGRLAVAKDIAVEAQNESKWKQLGELAMSSGKLDMAEECMRHAMDLSGLLLLYSSL 706
Cdd:pfam04053 303 KKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLST 382

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 238479136  707 GDADGMMKLAALAKEQGKNNVAFLCLFMLGQVEDCLHLLVESNRIPEAALMARSYLP 763
Cdd:pfam04053 383 GNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 17-297 9.38e-65

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: 219.51  E-value: 9.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  17 RVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVYNYNTMDKIKVFE 96
Cdd:cd00200   11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  97 AHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGwLCTQIFEGHSHYVMQVTFNPkdTNTF-ASASLDRTIKIWNLGSP 175
Cdd:cd00200   91 GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTG 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 176 DPNFTLDAHLKGVNCVDYFTGGDKpyLITGSDDHTAKVWDYQTKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRI 255
Cdd:cd00200  168 KCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 238479136 256 WHATTYRLENTLNYGLERVWAIGHIKGSRRVVIGYDEGSIMV 297
Cdd:cd00200  246 WDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
6-297 3.75e-58

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 205.15  E-value: 3.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136   6 EIKRKFAQRSERVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVYN 85
Cdd:COG2319  111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  86 YNTMDKIKVFEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGwLCTQIFEGHSHYVMQVTFNPkDTNTFASASLDR 165
Cdd:COG2319  191 LATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSP-DGRLLASGSADG 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 166 TIKIWNLGSPDPNFTLDAHLKGVNCVDyFTGGDKpYLITGSDDHTAKVWDYQTKSCVQTLEGHTHNVSAVSFHPELPIII 245
Cdd:COG2319  269 TVRLWDLATGELLRTLTGHSGGVNSVA-FSPDGK-LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLA 346

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 238479136 246 TGSEDGTVRIWHATTYRLENTLNYGLERVWAIGHIKGSRRVVIGYDEGSIMV 297
Cdd:COG2319  347 SGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 218-257 7.16e-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: 57.71  E-value: 7.16e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 238479136   218 TKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRIWH 257
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
219-256 9.23e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 54.66  E-value: 9.23e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 238479136  219 KSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRIW 256
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 109-266 3.33e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.86  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 109 PTLpyVLSSSDDMLIKLWDWEKGWLCTQIFEGHShyVMQVTFNPKDTNTFASASLDRTIKIWNLGSPD-PNFTLDAHLKG 187
Cdd:PLN00181 588 PTL--LASGSDDGSVKLWSINQGVSIGTIKTKAN--ICCVQFPSESGRSLAFGSADHKVYYYDLRNPKlPLCTMIGHSKT 663

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 188 VNCVDYFtggDKPYLITGSDDHTAKVWDYQ------TKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRIWHAT-- 259
Cdd:PLN00181 664 VSYVRFV---DSSTLVSSSTDNTLKLWDLSmsisgiNETPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKAfp 740

                        170
                 ....*....|.
gi 238479136 260 ----TYRLENT 266
Cdd:PLN00181 741 mpvlSYKFKTI 751
 
Name Accession Description Interval E-value
Coatomer_WDAD_beta-like cd22947
Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', ...
 304-777 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: 850.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 304 PVASMDNSGKIIWAKHNEIHTVNIKSVGADEVTDGERLPLAVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALAW 383
Cdd:cd22947    1 PAVSMDSSGKIIWAKHNEIQTANLKALDEEEDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALAW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 384 RNRSFGSALEFVWSSDG-EHAVRESSTKIKIFsKNFQEKKTVRPTFSAEHIFGGTLLTMCSSDFICFYDWAECRLIRRID 462
Cdd:cd22947   81 RNKAFGSALEFVWSSDSnYYAVRESSSSVKIF-KNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRID 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 463 VTVKNLYWADSGDLVAIASDTSFYILKFNRDIVSSYFDGGKQIDEEGIEDAFELLNETNERVRTGLWVGDCFIYTNSSWR 542
Cdd:cd22947  160 VEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSANR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 543 LNYCVGGEVTTMYHLDRPMYLLGYLANQSRVYLIDKEFNVIGYTLLLSLIEYKTLVMRGDLEQANEVLPSIPKEHHNSVA 622
Cdd:cd22947  240 LNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKVA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 623 HFLESRGMTEDALEVATDPDYRFELAIQLGRLAVAKDIAVEAQNESKWKQLGELAMSSGKLDMAEECMRHAMDLSGLLLL 702
Cdd:cd22947  320 RFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLLL 399

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238479136 703 YSSLGDADGMMKLAALAKEQGKNNVAFLCLFMLGQVEDCLHLLVESNRIPEAALMARSYLPSKVSEIVALWRNDL 777
Cdd:cd22947  400 YSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDL 474
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 319-763 0e+00

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 531.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  319 HNEIHTVNIKSVGAdevTDGERLPLAVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALAWRNRSFGSALEFVWSS 398
Cdd:pfam04053   1 ENEVRSYNIKGIEN---KDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  399 DGEHAVRESSTKIKIFsKNFQEK--KTVRPTFSAEHIFG---GTLLTMCSSDFICFYDWAECRLIRRIDVT-VKNLYWAD 472
Cdd:pfam04053  78 RNRFAVLEKSGTVKIF-KNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVSpVKYVIWSD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  473 SGDLVAIASDTSFYILKFNRDIVssyfdggkqidEEGIEDAFELLNETNERVRTGLWVGDCFIYTNSSwRLNYCVGGEVT 552
Cdd:pfam04053 157 DGELVALLSKDTVYILNYNLEAV-----------EDGVEDAFEVLHEISERVKSGAWDGDVFIYTTSN-HLKYLVNGDSG 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  553 TMYHLDRPMYLLGYLANQSRVYLIDKEFNVIGYTLLLSLIEYKTLVMRGDLEQ------ANEVLPsiPKEHHNSVAHFLE 626
Cdd:pfam04053 225 IIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEEvlriirASNLLP--PKDEGQKIIRYLE 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  627 SRGMTEDALEVATDPDYRFELAIQLGRLAVAKDIAVEAQNESKWKQLGELAMSSGKLDMAEECMRHAMDLSGLLLLYSSL 706
Cdd:pfam04053 303 KKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLST 382

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 238479136  707 GDADGMMKLAALAKEQGKNNVAFLCLFMLGQVEDCLHLLVESNRIPEAALMARSYLP 763
Cdd:pfam04053 383 GNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
Coatomer_WDAD cd22938
Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds ...
 304-775 2.46e-171

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: 506.07  E-value: 2.46e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 304 PVASMDNSGKIIWAKHNEiHTVNIKSVGADEVTDGERLPLAVKELGTCDLYPQSLKHNPNGRFVVVCGDGEYIIYTALAW 383
Cdd:cd22938    1 PAYSVDGNGKLHWVKHSE-QQADRFLRQLDFNSDGEKLVLVMKLRGSSKFPPQNMSHNPNGRFVLVCGDGEYDIYTAPAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 384 RNRSFGSALEFVWSSDG-EHAVRESSTKIKIFsKNFQE--KKTVRPTFSAEHIFGGTLLTMCSSDFICFYDWAECRLIRR 460
Cdd:cd22938   80 RNKSFGSAQTFVWVADSrFYALDRMHSSLKIK-KNFKEitSKIVPNCDEIFYAGTGNLLGVDSVDSITFFDWQNKRLLRR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 461 IDVTVKNLYWADSGDLVAIASDTSFYILKFNRDIVSSYFDGGKQIDEEGIEDAFELLNETNERVRTGLWVGDCFIYTNSS 540
Cdd:cd22938  159 IKIKVKYVIWSDDGELVAILAKHSIVILNYLSEKVLAAQETHEGVTEDGIERAFDVLCEIHERVKSGAWVGDVFIYTTSS 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 541 WRLNYCVGGEVTTMYHLDRPMYLLGYLANQSRVYLIDKEFNVIGYTLLLSLIEYKTLVMRGDLEQANEVLPSIPKEHHNS 620
Cdd:cd22938  239 NRLNYAVGGGHGIIAHLDLPMYLLGYKGNDNNVYLLDRECRPRVYTIDPTVLEFQTALIRRKYDMADEVLPMVRNAKRTR 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 621 VAHFLESRGMTEDALEVATDPDYRFELAIQLGRLAVAKDIAVEAQNESKWKQLGELAMSSGKLDMAEECMRHAMDLSGLL 700
Cdd:cd22938  319 VAHFLEKQGFKQQALVGSSDIAYLFELALPEGALKIAYQLAHFVKDEKKWFSLALECGSKCNFELALEAAKAANDWEKLG 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238479136 701 LLYSSLGDADGMMKLAALAKEQGKNNVAFLCLFMLGQVEDCLHLLVESNRIPEAALMARSYLPSKVSEIVALWRN 775
Cdd:cd22938  399 LLALLQGNHQIVEMLAQRAENFGKNNKAFFLYLITGKLRKMMKLLIIRKRDMEAAFLNATYLGDQVSERVRIWKE 473
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 17-297 9.38e-65

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: 219.51  E-value: 9.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  17 RVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVYNYNTMDKIKVFE 96
Cdd:cd00200   11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  97 AHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGwLCTQIFEGHSHYVMQVTFNPkdTNTF-ASASLDRTIKIWNLGSP 175
Cdd:cd00200   91 GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTG 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 176 DPNFTLDAHLKGVNCVDYFTGGDKpyLITGSDDHTAKVWDYQTKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRI 255
Cdd:cd00200  168 KCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 238479136 256 WHATTYRLENTLNYGLERVWAIGHIKGSRRVVIGYDEGSIMV 297
Cdd:cd00200  246 WDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
6-297 3.75e-58

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 205.15  E-value: 3.75e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136   6 EIKRKFAQRSERVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVYN 85
Cdd:COG2319  111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  86 YNTMDKIKVFEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGwLCTQIFEGHSHYVMQVTFNPkDTNTFASASLDR 165
Cdd:COG2319  191 LATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSP-DGRLLASGSADG 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 166 TIKIWNLGSPDPNFTLDAHLKGVNCVDyFTGGDKpYLITGSDDHTAKVWDYQTKSCVQTLEGHTHNVSAVSFHPELPIII 245
Cdd:COG2319  269 TVRLWDLATGELLRTLTGHSGGVNSVA-FSPDGK-LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLA 346

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 238479136 246 TGSEDGTVRIWHATTYRLENTLNYGLERVWAIGHIKGSRRVVIGYDEGSIMV 297
Cdd:COG2319  347 SGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
WD40 COG2319
WD40 repeat [General function prediction only];
15-260 1.02e-54

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 195.52  E-value: 1.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  15 SERVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVYNYNTMDKIKV 94
Cdd:COG2319  162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  95 FEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGwLCTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTIKIWNLGS 174
Cdd:COG2319  242 LTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG-ELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLAT 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 175 PDPNFTLDAHLKGVNCVDYFTGGDkpYLITGSDDHTAKVWDYQTKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVR 254
Cdd:COG2319  320 GKLLRTLTGHTGAVRSVAFSPDGK--TLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVR 397


                 ....*.
gi 238479136 255 IWHATT 260
Cdd:COG2319  398 LWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
3-297 2.35e-54

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 194.36  E-value: 2.35e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136   3 LRLEIKRKFAQRSERVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIR 82
Cdd:COG2319   66 AAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVR 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  83 VYNYNTMDKIKVFEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGWlCTQIFEGHSHYVMQVTFNPkDTNTFASAS 162
Cdd:COG2319  146 LWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGK-LLRTLTGHTGAVRSVAFSP-DGKLLASGS 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 163 LDRTIKIWNLGSPDPNFTLDAHLKGVNCVDYFTGGDkpYLITGSDDHTAKVWDYQTKSCVQTLEGHTHNVSAVSFHPELP 242
Cdd:COG2319  224 ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGR--LLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGK 301

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 238479136 243 IIITGSEDGTVRIWHATTYRLENTLNYGLERVWAIGHIKGSRRVVIGYDEGSIMV 297
Cdd:COG2319  302 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
WD40 COG2319
WD40 repeat [General function prediction only];
11-297 3.39e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 185.50  E-value: 3.39e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  11 FAQRSERVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVYNYNTMD 90
Cdd:COG2319   32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  91 KIKVFEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGWlCTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTIKIW 170
Cdd:COG2319  112 LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK-LLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGTVRLW 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 171 NLGSPDPNFTLDAHLKGVNCVDYFTGGDkpYLITGSDDHTAKVWDYQTKSCVQTLEGHTHNVSAVSFHPELPIIITGSED 250
Cdd:COG2319  190 DLATGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSAD 267

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 238479136 251 GTVRIWHATTYRLENTLNYGLERVWAIGHIKGSRRVVIGYDEGSIMV 297
Cdd:COG2319  268 GTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRL 314
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 6-215 1.80e-45

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 165.20  E-value: 1.80e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136   6 EIKRKFAQRSERVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVYN 85
Cdd:cd00200   84 ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWD 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  86 YNTMDKIKVFEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGWlCTQIFEGHSHYVMQVTFNPkDTNTFASASLDR 165
Cdd:cd00200  164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK-CLGTLRGHENGVNSVAFSP-DGYLLASGSEDG 241

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 238479136 166 TIKIWNLGSPDPNFTLDAHLKGVNCVDYFTggDKPYLITGSDDHTAKVWD 215
Cdd:cd00200  242 TIRVWDLRTGECVQTLSGHTNSVTSLAWSP--DGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 92-297 1.46e-44

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 162.89  E-value: 1.46e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  92 IKVFEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWEKGWL-------------------------------------- 133
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELlrtlkghtgpvrdvaasadgtylasgssdktirlwdle 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 134 ---CTQIFEGHSHYVMQVTFNPKDTnTFASASLDRTIKIWNLGSPDPNFTLDAHLKGVNCVDYftGGDKPYLITGSDDHT 210
Cdd:cd00200   82 tgeCVRTLTGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAF--SPDGTFVASSSQDGT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 211 AKVWDYQTKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRIWHATTYRLENTLNYGLERVWAIGHIKGSRRVVIGY 290
Cdd:cd00200  159 IKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGS 238


                 ....*..
gi 238479136 291 DEGSIMV 297
Cdd:cd00200  239 EDGTIRV 245
WD40 COG2319
WD40 repeat [General function prediction only];
22-297 8.97e-44

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 163.93  E-value: 8.97e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136  22 DLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVYNYNTMDKIKVFEAHADY 101
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 102 IRCVAVHPTLPYVLSSSDDMLIKLWDWEKGwLCTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTIKIWNLGSPDPNFTL 181
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLATG-LLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLATGKLLRTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 182 DAHLKGVNCVDYFTGGDkpYLITGSDDHTAKVWDYQTKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRIWHATTY 261
Cdd:COG2319  159 TGHSGAVTSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG 236

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 238479136 262 RLENTLNYGLERVWAIGHIKGSRRVVIGYDEGSIMV 297
Cdd:COG2319  237 KLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRL 272
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 134-297 4.26e-37

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 141.32  E-value: 4.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 134 CTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTIKIWNLGSPDPNFTLDAHLKGVNCVDYFtgGDKPYLITGSDDHTAKV 213
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAS--ADGTYLASGSSDKTIRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 214 WDYQTKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRIWHATTYRLENTLNYGLERVWAIGHIKGSRRVVIGYDEG 293
Cdd:cd00200   78 WDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157


                 ....
gi 238479136 294 SIMV 297
Cdd:cd00200  158 TIKL 161
Coatomer_WDAD_alpha cd22948
Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called ...
 355-761 7.09e-26

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: 111.84  E-value: 7.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 355 PQSLKHNPNGRFVVVCGDGE------YIIYTALAWRN----RSFGSALEFVWSSDGEHAVRESSTKIKIfsKNFQEK--K 422
Cdd:cd22948   46 PRSLSYNPAENAVLVTSDADggsyelYTLPKDSSGAPekpeSKRGSGLSAVFVARNRFAVLDKSGTILI--KNLENEvtK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 423 TVRPTFSAEHIFGGT----LLTmcSSDFICFYDWAECRLIRRIDVT-VKNLYWADSGDLVAIASDTSFYIlkFNRDivss 497
Cdd:cd22948  124 KIKPPPNVDKIFYAGtgrvLLR--SEDKVILFDVQQKRVLAEVKVPkVKYVVWSKDMSHVALLSKHSITI--ATKK---- 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 498 yfdggkqideegiedaFELLNETNE--RVRTGLWVGD-CFIYTNSSwRLNYC-VGGEVTTMYHLDRPMYLLGylANQSRV 573
Cdd:cd22948  196 ----------------LEQLCSVHEtiRIKSGAWDESgVLIYTTLN-HIKYLlPNGDSGIIRTLDSPIYLTR--VKGNTV 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 574 YLIDKEFNVigYTLLLSLIEY--KTLVMRGDLEqanEVLpSIPKEHH---NSVAHFLESRGMTEDALEVATDPDYRFELA 648
Cdd:cd22948  257 YCLDREGKV--RVLEIDPTEYlfKLALINKNYD---EVL-RIIRSSKlvgQSIIAYLQKKGYPEIALHFVKDPKTRFNLA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 649 IQLGRLAVAKDIAVEAQNESKWKQLGELAMSSGKLDMAEECMRHAMDLSGLLLLYSSLGDADGMMKLAALAKEQGKNNVA 728
Cdd:cd22948  331 LECGNLEVALEAAKELDDPECWERLAEEALRQGNHQIVEMAYQKTKNFDKLSFLYLITGNLEKLRKMLKIAEKRGDVMSR 410

                        410       420       430
                 ....*....|....*....|....*....|...
gi 238479136 729 FLCLFMLGQVEDCLHLLVESNRIPEAALMARSY 761
Cdd:cd22948  411 FQNALYLGDVEERVKILKEAGQLPLAYLTAKTH 443
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-127 9.00e-18

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: 84.69  E-value: 9.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136   5 LEIKRKFAQRSERVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVY 84
Cdd:cd00200  167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 238479136  85 NYNTMDKIKVFEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWD 127
Cdd:cd00200  247 DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
6-129 8.07e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 77.64  E-value: 8.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136   6 EIKRKFAQRSERVKSVDLHPTEPWILASLYSGTLCIWNYQTQTMVKSFDVTELPVRSAKFIARKQWVVAGADDMFIRVYN 85
Cdd:COG2319  279 ELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWD 358

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 238479136  86 YNTMDKIKVFEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWDWE 129
Cdd:COG2319  359 LATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 218-257 7.16e-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: 57.71  E-value: 7.16e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 238479136   218 TKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRIWH 257
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 221-482 1.08e-10

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: 63.51  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 221 CVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRIWHATTYRLENTLnyglervwaIGHIKGSRRVVIGYDegsimvklG 300
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL---------KGHTGPVRDVAASAD--------G 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 301 REIPVASMDNSGKIIWAKHNEI------HTVNIKSV------------GAD------EVTDGErlplAVKELGTCDLYPQ 356
Cdd:cd00200   64 TYLASGSSDKTIRLWDLETGECvrtltgHTSYVSSVafspdgrilsssSRDktikvwDVETGK----CLTTLRGHTDWVN 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 357 SLKHNPNGRFVVVCG-DGeyiiyTALAWRNRSFGSALEFV----------WSSDGEHAVRESSTK-IKIFS-KNFQEKKT 423
Cdd:cd00200  140 SVAFSPDGTFVASSSqDG-----TIKLWDLRTGKCVATLTghtgevnsvaFSPDGEKLLSSSSDGtIKLWDlSTGKCLGT 214

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238479136 424 VR----PTFSAEHIFGGTLLTMCSSDF-ICFYDWAECRLIRRI---DVTVKNLYWADSGDLVAIASD 482
Cdd:cd00200  215 LRghenGVNSVAFSPDGYLLASGSEDGtIRVWDLRTGECVQTLsghTNSVTSLAWSPDGKRLASGSA 281
WD40 pfam00400
WD domain, G-beta repeat;
219-256 9.23e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 54.66  E-value: 9.23e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 238479136  219 KSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRIW 256
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 88-127 2.30e-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: 2.30e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 238479136    88 TMDKIKVFEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWD 127
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 134-171 3.27e-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: 47.31  E-value: 3.27e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 238479136   134 CTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTIKIWN 171
Cdd:smart00320   4 LLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
92-127 8.17e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.18  E-value: 8.17e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 238479136   92 IKVFEAHADYIRCVAVHPTLPYVLSSSDDMLIKLWD 127
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
134-171 1.58e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.41  E-value: 1.58e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 238479136  134 CTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTIKIWN 171
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 109-266 3.33e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.86  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 109 PTLpyVLSSSDDMLIKLWDWEKGWLCTQIFEGHShyVMQVTFNPKDTNTFASASLDRTIKIWNLGSPD-PNFTLDAHLKG 187
Cdd:PLN00181 588 PTL--LASGSDDGSVKLWSINQGVSIGTIKTKAN--ICCVQFPSESGRSLAFGSADHKVYYYDLRNPKlPLCTMIGHSKT 663

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 188 VNCVDYFtggDKPYLITGSDDHTAKVWDYQ------TKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRIWHAT-- 259
Cdd:PLN00181 664 VSYVRFV---DSSTLVSSSTDNTLKLWDLSmsisgiNETPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKAfp 740

                        170
                 ....*....|.
gi 238479136 260 ----TYRLENT 266
Cdd:PLN00181 741 mpvlSYKFKTI 751
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 179-215 2.57e-05

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 41.91  E-value: 2.57e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 238479136   179 FTLDAHLKGVNCVDYFtgGDKPYLITGSDDHTAKVWD 215
Cdd:smart00320   6 KTLKGHTGPVTSVAFS--PDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
177-215 2.71e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 41.95  E-value: 2.71e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 238479136  177 PNFTLDAHLKGVNCVDYFTggDKPYLITGSDDHTAKVWD 215
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSP--DGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 137-255 5.12e-05

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 46.81  E-value: 5.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238479136 137 IFEGHSHYVMQVTFNPKDTNTFASASLDRTIKIWNL-------GSPDPNFTLDAHLKGVNCVDyFTGGDKPYLITGSDDH 209
Cdd:PTZ00421  70 ILLGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIpeegltqNISDPIVHLQGHTKKVGIVS-FHPSAMNVLASAGADM 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 238479136 210 TAKVWDYQTKSCVQTLEGHTHNVSAVSFHPELPIIITGSEDGTVRI 255
Cdd:PTZ00421 149 VVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNI 194
 
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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