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Conserved domains on  [gi|24655452|ref|NP_728648|]
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coat protein (coatomer) alpha, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Coatomer_WDAD_alpha cd22948
Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called ...
 327-773 0e+00

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: 791.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  327 PAYAVHGNILYYVKERFLRKLDFTTTKDTVVMQLR-----PGKSPVYSMSYNPALNAVLICTRTnnlENSTYDLCQIPKD 401
Cdd:cd22948    1 PAFAVHGNSLYYVKDRKLRVYDFSSGSRVSVPVLSlrgrgGSNQPPRSLSYNPAENAVLVTSDA---DGGSYELYTLPKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  402 TESQSE-SDSKRSSGITAIWVARNRFAVLDRNQQLVIKNFKNEVTKKL--PTFCEEIFYAGTGMLLIRDPEFVTLYEVQR 478
Cdd:cd22948   78 SSGAPEkPESKRGSGLSAVFVARNRFAVLDKSGTILIKNLENEVTKKIkpPPNVDKIFYAGTGRVLLRSEDKVILFDVQQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  479 LVSVGSIKLAKCRYVVWSPDMSLVALLCKHSVTICDRRLQYLCTVQENCRVKSGAWDESGVFIYTTSNHIKYAITNGDHG 558
Cdd:cd22948  158 KRVLAEVKVPKVKYVVWSKDMSHVALLSKHSITIATKKLEQLCSVHETIRIKSGAWDESGVLIYTTLNHIKYLLPNGDSG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  559 IIRTLDLPIYLTRVKGNQVFCLDRECRTRVLHIDPTEYKFKLALIQRKYDEVLHMVRNARLVGQSIIAYLQQKGYPEVAL 638
Cdd:cd22948  238 IIRTLDSPIYLTRVKGNTVYCLDREGKVRVLEIDPTEYLFKLALINKNYDEVLRIIRSSKLVGQSIIAYLQKKGYPEIAL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  639 HFVKDEKTRFGLALECGNIEIALEAAKALDDKDCWDRLGQSALLQGNHQVVEMCYQRTKNFDKLSFLYLITGNLEKLKKM 718
Cdd:cd22948  318 HFVKDPKTRFNLALECGNLEVALEAAKELDDPECWERLAEEALRQGNHQIVEMAYQKTKNFDKLSFLYLITGNLEKLRKM 397

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24655452  719 NKIAEIRKDVSAQYQGALLLGDVKERVNILKNCGQLSLAYLTAATHGFDELTESL 773
Cdd:cd22948  398 LKIAEKRGDVMSRFQNALYLGDVEERVKILKEAGQLPLAYLTAKTHGLEELAEEI 452
COPI_C pfam06957
Coatomer (COPI) alpha subunit C-terminus; This family represents the C-terminus (approximately ...
 815-1228 0e+00

Coatomer (COPI) alpha subunit C-terminus; This family represents the C-terminus (approximately 500 residues) of the eukaryotic coatomer alpha subunit. Coatomer (COPI) is a large cytosolic protein complex which forms a coat around vesicles budding from the Golgi apparatus. Such coatomer-coated vesicles have been proposed to play a role in many distinct steps of intracellular transport. Note that many family members also contain the pfam04053 domain.


:

Pssm-ID: 462050  Cd Length: 402  Bit Score: 640.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    815 GFFEGAMVTRAGSSATArqaLNIN----------ADAAL-LDEHNGGGDgwgadadlgldedgddeMHDALSNDGDGGAG 883
Cdd:pfam06957    1 GFFEGALAAAGGGSAAA---VDEDddeaagagwgDDADLdLDEANGGIE-----------------DEDDDEEEGEDGGD 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    884 GEEGAGWDVgdDDLVVPEELASKIKASALDSNYYAAPNKGLSPAQQWANNSPLVLDHVKAGSFETAFRLLHDQLGVVNFQ 963
Cdd:pfam06957   61 DDEEGGWDV--EDLELPPELDVGAAAGAARSGYFVAPTPGVPPSQIWTNNSQLAVDHAAAGSFETAMRLLHRQLGVVNFA 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    964 PFKTLFLQNYACSRTSYTANPNLQSLSGYPLRNYSETNIKLQRPAVGIKLNDLVARLQAGYQLTTSGKFSEAVEKFHSIL 1043
Cdd:pfam06957  139 PLKPLFLDAYAGSRTSLRGLPSLPSLPGYPERNWSEDGAKNGPPALVYKLSQLEERLQAAYKLTTEGKFSEALRKFRSIL 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   1044 ISIPLLVVDTKLDAAEAQQLLRICAEYIVGLKMETVRKGMPKStLEEQKRLCEMAAYFTHCKLQPVHQILTLRTALNMFF 1123
Cdd:pfam06957  219 HSIPLLVVDSKQEVDEVQQLITICREYIVGLRMETKRKELPKS-LDDQKRQAELAAYFTHCNLQPVHLILTLRTAMNLFF 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   1124 KLKNYKTAASFARRLLELAPRPDVAQQVRKILQACEVNPVDEHQLQYEEFNPFTICGISWKPLYRGKPEVTCPFCSSSFD 1203
Cdd:pfam06957  298 KLKNFKTAASFARRLLELGPPPKVAQQARKVLQACEKNPTDAHQLNYDEHNPFVVCGATFVPIYRGKPDVKCPYCGASYV 377

                          410       420
                   ....*....|....*....|....*
gi 24655452   1204 PQFKGNLCTVCEVSQIGKDSIGLRI 1228
Cdd:pfam06957  378 PEFKGQVCTVCQVAEIGKDASGLRI 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-321 1.88e-72

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: 243.40  E-value: 1.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    5 FESKSARVKGLSFHPKRPWILVSLHSGVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWNYKQRR 84
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   85 CIFTLLAHLDYVRTVAFHHEYPWILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWDI 164
Cdd:cd00200   85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  165 SGLRkknvapgpgglddhlkghpgatdlfgqadavVKHVLEGHDRGVNWASFHPTLPLIVSGADDRLVKLWRMNeyKAWE 244
Cdd:cd00200  165 RTGK-------------------------------CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS--TGKC 211

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24655452  245 VDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWDMTKRQCLFTFRRDNERFWILTAHPTLN-LFAAGHDGGMVVFK 321
Cdd:cd00200  212 LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKrLASGSADGTIRIWD 289
 
Name Accession Description Interval E-value
Coatomer_WDAD_alpha cd22948
Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called ...
 327-773 0e+00

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: 791.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  327 PAYAVHGNILYYVKERFLRKLDFTTTKDTVVMQLR-----PGKSPVYSMSYNPALNAVLICTRTnnlENSTYDLCQIPKD 401
Cdd:cd22948    1 PAFAVHGNSLYYVKDRKLRVYDFSSGSRVSVPVLSlrgrgGSNQPPRSLSYNPAENAVLVTSDA---DGGSYELYTLPKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  402 TESQSE-SDSKRSSGITAIWVARNRFAVLDRNQQLVIKNFKNEVTKKL--PTFCEEIFYAGTGMLLIRDPEFVTLYEVQR 478
Cdd:cd22948   78 SSGAPEkPESKRGSGLSAVFVARNRFAVLDKSGTILIKNLENEVTKKIkpPPNVDKIFYAGTGRVLLRSEDKVILFDVQQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  479 LVSVGSIKLAKCRYVVWSPDMSLVALLCKHSVTICDRRLQYLCTVQENCRVKSGAWDESGVFIYTTSNHIKYAITNGDHG 558
Cdd:cd22948  158 KRVLAEVKVPKVKYVVWSKDMSHVALLSKHSITIATKKLEQLCSVHETIRIKSGAWDESGVLIYTTLNHIKYLLPNGDSG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  559 IIRTLDLPIYLTRVKGNQVFCLDRECRTRVLHIDPTEYKFKLALIQRKYDEVLHMVRNARLVGQSIIAYLQQKGYPEVAL 638
Cdd:cd22948  238 IIRTLDSPIYLTRVKGNTVYCLDREGKVRVLEIDPTEYLFKLALINKNYDEVLRIIRSSKLVGQSIIAYLQKKGYPEIAL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  639 HFVKDEKTRFGLALECGNIEIALEAAKALDDKDCWDRLGQSALLQGNHQVVEMCYQRTKNFDKLSFLYLITGNLEKLKKM 718
Cdd:cd22948  318 HFVKDPKTRFNLALECGNLEVALEAAKELDDPECWERLAEEALRQGNHQIVEMAYQKTKNFDKLSFLYLITGNLEKLRKM 397

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24655452  719 NKIAEIRKDVSAQYQGALLLGDVKERVNILKNCGQLSLAYLTAATHGFDELTESL 773
Cdd:cd22948  398 LKIAEKRGDVMSRFQNALYLGDVEERVKILKEAGQLPLAYLTAKTHGLEELAEEI 452
COPI_C pfam06957
Coatomer (COPI) alpha subunit C-terminus; This family represents the C-terminus (approximately ...
 815-1228 0e+00

Coatomer (COPI) alpha subunit C-terminus; This family represents the C-terminus (approximately 500 residues) of the eukaryotic coatomer alpha subunit. Coatomer (COPI) is a large cytosolic protein complex which forms a coat around vesicles budding from the Golgi apparatus. Such coatomer-coated vesicles have been proposed to play a role in many distinct steps of intracellular transport. Note that many family members also contain the pfam04053 domain.


Pssm-ID: 462050  Cd Length: 402  Bit Score: 640.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    815 GFFEGAMVTRAGSSATArqaLNIN----------ADAAL-LDEHNGGGDgwgadadlgldedgddeMHDALSNDGDGGAG 883
Cdd:pfam06957    1 GFFEGALAAAGGGSAAA---VDEDddeaagagwgDDADLdLDEANGGIE-----------------DEDDDEEEGEDGGD 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    884 GEEGAGWDVgdDDLVVPEELASKIKASALDSNYYAAPNKGLSPAQQWANNSPLVLDHVKAGSFETAFRLLHDQLGVVNFQ 963
Cdd:pfam06957   61 DDEEGGWDV--EDLELPPELDVGAAAGAARSGYFVAPTPGVPPSQIWTNNSQLAVDHAAAGSFETAMRLLHRQLGVVNFA 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    964 PFKTLFLQNYACSRTSYTANPNLQSLSGYPLRNYSETNIKLQRPAVGIKLNDLVARLQAGYQLTTSGKFSEAVEKFHSIL 1043
Cdd:pfam06957  139 PLKPLFLDAYAGSRTSLRGLPSLPSLPGYPERNWSEDGAKNGPPALVYKLSQLEERLQAAYKLTTEGKFSEALRKFRSIL 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   1044 ISIPLLVVDTKLDAAEAQQLLRICAEYIVGLKMETVRKGMPKStLEEQKRLCEMAAYFTHCKLQPVHQILTLRTALNMFF 1123
Cdd:pfam06957  219 HSIPLLVVDSKQEVDEVQQLITICREYIVGLRMETKRKELPKS-LDDQKRQAELAAYFTHCNLQPVHLILTLRTAMNLFF 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   1124 KLKNYKTAASFARRLLELAPRPDVAQQVRKILQACEVNPVDEHQLQYEEFNPFTICGISWKPLYRGKPEVTCPFCSSSFD 1203
Cdd:pfam06957  298 KLKNFKTAASFARRLLELGPPPKVAQQARKVLQACEKNPTDAHQLNYDEHNPFVVCGATFVPIYRGKPDVKCPYCGASYV 377

                          410       420
                   ....*....|....*....|....*
gi 24655452   1204 PQFKGNLCTVCEVSQIGKDSIGLRI 1228
Cdd:pfam06957  378 PEFKGQVCTVCQVAEIGKDASGLRI 402
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 353-765 1.66e-168

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 506.77  E-value: 1.66e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    353 KDTVVMQLR-PGKSPVY--SMSYNPALNAVLICtrtnnlENSTYDLCQipkdteSQSESDSKRSSGITAIWVARNRFAVL 429
Cdd:pfam04053   17 GELLSLSLKeLGSVEIYpqTLSHNPNGRFVLVC------GDGEYIIYT------ALAWRNKAYGKGLDFVWVSRNRFAVL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    430 DRNQQLVI-KNFKNEVTK--KLPTFCEEIFYAGTGMLLIRDPE-FVTLYEVQRLVSVGSIKLAKCRYVVWSPDMSLVALL 505
Cdd:pfam04053   85 EKSGTVKIfKNFKESVTKsiKLPYSVDKIFGGGPGSLLGVKSEgSLSFYDWEQGKLVRRIDVSPVKYVIWSDDGELVALL 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    506 CKHSVTICDRRLQY--------LCTVQE-NCRVKSGAWDESgVFIYTTSNHIKYaITNGDHGIIRTLDLPIYLTRVKG-- 574
Cdd:pfam04053  165 SKDTVYILNYNLEAvedgvedaFEVLHEiSERVKSGAWDGD-VFIYTTSNHLKY-LVNGDSGIIKTLDKTLYLLGYLGke 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    575 NQVFCLDRECRTRVLHIDPTEYKFKLALIQRKYDEVLHMVRNARLV-----GQSIIAYLQQKGYPEVALHFVKDEKTRFG 649
Cdd:pfam04053  243 NRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEEVLRIIRASNLLppkdeGQKIIRYLEKKGYPEIALQFVQDPDTRFD 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    650 LALECGNIEIALEAAKALDDKDCWDRLGQSALLQGNHQVVEMCYQRTKNFDKLSFLYLITGNLEKLKKMNKIAEIRKDVS 729
Cdd:pfam04053  323 LALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLSTGNMEKLKKLAKIAEKRGDYN 402

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 24655452    730 AQYQGALLLGDVKERVNILKNCGQLSLAYLTAATHG 765
Cdd:pfam04053  403 SAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYG 438
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-321 1.88e-72

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: 243.40  E-value: 1.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    5 FESKSARVKGLSFHPKRPWILVSLHSGVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWNYKQRR 84
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   85 CIFTLLAHLDYVRTVAFHHEYPWILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWDI 164
Cdd:cd00200   85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  165 SGLRkknvapgpgglddhlkghpgatdlfgqadavVKHVLEGHDRGVNWASFHPTLPLIVSGADDRLVKLWRMNeyKAWE 244
Cdd:cd00200  165 RTGK-------------------------------CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS--TGKC 211

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24655452  245 VDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWDMTKRQCLFTFRRDNERFWILTAHPTLN-LFAAGHDGGMVVFK 321
Cdd:cd00200  212 LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKrLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
5-318 4.07e-56

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 200.52  E-value: 4.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    5 FESKSARVKGLSFHPKRPWILVSLHSGVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWNYKQRR 84
Cdd:COG2319   74 LLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   85 CIFTLLAHLDYVRTVAFHHEYPWILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWDI 164
Cdd:COG2319  154 LLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  165 SGLRKKNVAPGPGGL--------DDHL---KGHPGATDLFGQADAVVKHVLEGHDRGVNWASFHPTLPLIVSGADDRLVK 233
Cdd:COG2319  234 ATGKLLRTLTGHSGSvrsvafspDGRLlasGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVR 313

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  234 LWRMNEYKawEVDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWDMTKRQCLFTFRRDNERFWILTAHPTLNLFAAGH 313
Cdd:COG2319  314 LWDLATGK--LLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGS 391


                 ....*
gi 24655452  314 DGGMV 318
Cdd:COG2319  392 ADGTV 396
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 124-163 1.08e-09

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: 54.63  E-value: 1.08e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 24655452     124 SRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWD 163
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
125-163 1.47e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 51.58  E-value: 1.47e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 24655452    125 RNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWD 163
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 31-165 1.30e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 56.25  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    31 GVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMP-LFVSGGDDYKIKVWNYKQRRCIFTLLAHLDyVRTVAFHHEYPWIL 109
Cdd:PLN00181  555 GVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPtLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFPSESGRSL 633

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   110 S-ASDDQtiRIWNWQSRN---CICVLTGHNHYVMCAQFHPTEdQIVSASLDQTVRVWDIS 165
Cdd:PLN00181  634 AfGSADH--KVYYYDLRNpklPLCTMIGHSKTVSYVRFVDSS-TLVSSSTDNTLKLWDLS 690
 
Name Accession Description Interval E-value
Coatomer_WDAD_alpha cd22948
Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called ...
 327-773 0e+00

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: 791.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  327 PAYAVHGNILYYVKERFLRKLDFTTTKDTVVMQLR-----PGKSPVYSMSYNPALNAVLICTRTnnlENSTYDLCQIPKD 401
Cdd:cd22948    1 PAFAVHGNSLYYVKDRKLRVYDFSSGSRVSVPVLSlrgrgGSNQPPRSLSYNPAENAVLVTSDA---DGGSYELYTLPKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  402 TESQSE-SDSKRSSGITAIWVARNRFAVLDRNQQLVIKNFKNEVTKKL--PTFCEEIFYAGTGMLLIRDPEFVTLYEVQR 478
Cdd:cd22948   78 SSGAPEkPESKRGSGLSAVFVARNRFAVLDKSGTILIKNLENEVTKKIkpPPNVDKIFYAGTGRVLLRSEDKVILFDVQQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  479 LVSVGSIKLAKCRYVVWSPDMSLVALLCKHSVTICDRRLQYLCTVQENCRVKSGAWDESGVFIYTTSNHIKYAITNGDHG 558
Cdd:cd22948  158 KRVLAEVKVPKVKYVVWSKDMSHVALLSKHSITIATKKLEQLCSVHETIRIKSGAWDESGVLIYTTLNHIKYLLPNGDSG 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  559 IIRTLDLPIYLTRVKGNQVFCLDRECRTRVLHIDPTEYKFKLALIQRKYDEVLHMVRNARLVGQSIIAYLQQKGYPEVAL 638
Cdd:cd22948  238 IIRTLDSPIYLTRVKGNTVYCLDREGKVRVLEIDPTEYLFKLALINKNYDEVLRIIRSSKLVGQSIIAYLQKKGYPEIAL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  639 HFVKDEKTRFGLALECGNIEIALEAAKALDDKDCWDRLGQSALLQGNHQVVEMCYQRTKNFDKLSFLYLITGNLEKLKKM 718
Cdd:cd22948  318 HFVKDPKTRFNLALECGNLEVALEAAKELDDPECWERLAEEALRQGNHQIVEMAYQKTKNFDKLSFLYLITGNLEKLRKM 397

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 24655452  719 NKIAEIRKDVSAQYQGALLLGDVKERVNILKNCGQLSLAYLTAATHGFDELTESL 773
Cdd:cd22948  398 LKIAEKRGDVMSRFQNALYLGDVEERVKILKEAGQLPLAYLTAKTHGLEELAEEI 452
COPI_C pfam06957
Coatomer (COPI) alpha subunit C-terminus; This family represents the C-terminus (approximately ...
 815-1228 0e+00

Coatomer (COPI) alpha subunit C-terminus; This family represents the C-terminus (approximately 500 residues) of the eukaryotic coatomer alpha subunit. Coatomer (COPI) is a large cytosolic protein complex which forms a coat around vesicles budding from the Golgi apparatus. Such coatomer-coated vesicles have been proposed to play a role in many distinct steps of intracellular transport. Note that many family members also contain the pfam04053 domain.


Pssm-ID: 462050  Cd Length: 402  Bit Score: 640.49  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    815 GFFEGAMVTRAGSSATArqaLNIN----------ADAAL-LDEHNGGGDgwgadadlgldedgddeMHDALSNDGDGGAG 883
Cdd:pfam06957    1 GFFEGALAAAGGGSAAA---VDEDddeaagagwgDDADLdLDEANGGIE-----------------DEDDDEEEGEDGGD 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    884 GEEGAGWDVgdDDLVVPEELASKIKASALDSNYYAAPNKGLSPAQQWANNSPLVLDHVKAGSFETAFRLLHDQLGVVNFQ 963
Cdd:pfam06957   61 DDEEGGWDV--EDLELPPELDVGAAAGAARSGYFVAPTPGVPPSQIWTNNSQLAVDHAAAGSFETAMRLLHRQLGVVNFA 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    964 PFKTLFLQNYACSRTSYTANPNLQSLSGYPLRNYSETNIKLQRPAVGIKLNDLVARLQAGYQLTTSGKFSEAVEKFHSIL 1043
Cdd:pfam06957  139 PLKPLFLDAYAGSRTSLRGLPSLPSLPGYPERNWSEDGAKNGPPALVYKLSQLEERLQAAYKLTTEGKFSEALRKFRSIL 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   1044 ISIPLLVVDTKLDAAEAQQLLRICAEYIVGLKMETVRKGMPKStLEEQKRLCEMAAYFTHCKLQPVHQILTLRTALNMFF 1123
Cdd:pfam06957  219 HSIPLLVVDSKQEVDEVQQLITICREYIVGLRMETKRKELPKS-LDDQKRQAELAAYFTHCNLQPVHLILTLRTAMNLFF 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   1124 KLKNYKTAASFARRLLELAPRPDVAQQVRKILQACEVNPVDEHQLQYEEFNPFTICGISWKPLYRGKPEVTCPFCSSSFD 1203
Cdd:pfam06957  298 KLKNFKTAASFARRLLELGPPPKVAQQARKVLQACEKNPTDAHQLNYDEHNPFVVCGATFVPIYRGKPDVKCPYCGASYV 377

                          410       420
                   ....*....|....*....|....*
gi 24655452   1204 PQFKGNLCTVCEVSQIGKDSIGLRI 1228
Cdd:pfam06957  378 PEFKGQVCTVCQVAEIGKDASGLRI 402
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 353-765 1.66e-168

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 506.77  E-value: 1.66e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    353 KDTVVMQLR-PGKSPVY--SMSYNPALNAVLICtrtnnlENSTYDLCQipkdteSQSESDSKRSSGITAIWVARNRFAVL 429
Cdd:pfam04053   17 GELLSLSLKeLGSVEIYpqTLSHNPNGRFVLVC------GDGEYIIYT------ALAWRNKAYGKGLDFVWVSRNRFAVL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    430 DRNQQLVI-KNFKNEVTK--KLPTFCEEIFYAGTGMLLIRDPE-FVTLYEVQRLVSVGSIKLAKCRYVVWSPDMSLVALL 505
Cdd:pfam04053   85 EKSGTVKIfKNFKESVTKsiKLPYSVDKIFGGGPGSLLGVKSEgSLSFYDWEQGKLVRRIDVSPVKYVIWSDDGELVALL 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    506 CKHSVTICDRRLQY--------LCTVQE-NCRVKSGAWDESgVFIYTTSNHIKYaITNGDHGIIRTLDLPIYLTRVKG-- 574
Cdd:pfam04053  165 SKDTVYILNYNLEAvedgvedaFEVLHEiSERVKSGAWDGD-VFIYTTSNHLKY-LVNGDSGIIKTLDKTLYLLGYLGke 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    575 NQVFCLDRECRTRVLHIDPTEYKFKLALIQRKYDEVLHMVRNARLV-----GQSIIAYLQQKGYPEVALHFVKDEKTRFG 649
Cdd:pfam04053  243 NRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEEVLRIIRASNLLppkdeGQKIIRYLEKKGYPEIALQFVQDPDTRFD 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    650 LALECGNIEIALEAAKALDDKDCWDRLGQSALLQGNHQVVEMCYQRTKNFDKLSFLYLITGNLEKLKKMNKIAEIRKDVS 729
Cdd:pfam04053  323 LALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLSTGNMEKLKKLAKIAEKRGDYN 402

                          410       420       430
                   ....*....|....*....|....*....|....*.
gi 24655452    730 AQYQGALLLGDVKERVNILKNCGQLSLAYLTAATHG 765
Cdd:pfam04053  403 SAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYG 438
Coatomer_WDAD cd22938
Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds ...
 327-751 4.49e-122

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: 385.89  E-value: 4.49e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  327 PAYAVHGN-ILYYVK------ERFLRKLDFTT--TKDTVVMQLRPG-KSPVYSMSYNPALNAVLICTRtnnlenSTYDLC 396
Cdd:cd22938    1 PAYSVDGNgKLHWVKhseqqaDRFLRQLDFNSdgEKLVLVMKLRGSsKFPPQNMSHNPNGRFVLVCGD------GEYDIY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  397 QIPKdtesqsesdSKRSSG---ITAIWVARNRFAVLDR-NQQLVIKNFKNEVTKKLPTFCEEIFYAGTGMLLIRD-PEFV 471
Cdd:cd22938   75 TAPA---------GRNKSFgsaQTFVWVADSRFYALDRmHSSLKIKKNFKEITSKIVPNCDEIFYAGTGNLLGVDsVDSI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  472 TLYEVQRLVSVGSIKLaKCRYVVWSPDMSLVALLCKHSVTIC----------------------DRRLQYLCTVQEncRV 529
Cdd:cd22938  146 TFFDWQNKRLLRRIKI-KVKYVIWSDDGELVAILAKHSIVILnylsekvlaaqethegvtedgiERAFDVLCEIHE--RV 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  530 KSGAWDEsGVFIYTT-SNHIKYAITnGDHGIIRTLDLPIYLTRVKG--NQVFCLDRECRTRVLHIDPTEYKFKLALIQRK 606
Cdd:cd22938  223 KSGAWVG-DVFIYTTsSNRLNYAVG-GGHGIIAHLDLPMYLLGYKGndNNVYLLDRECRPRVYTIDPTVLEFQTALIRRK 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  607 YD---EVLHMVRNAR-----------------LVGQSIIAYLQQKGYPEVAL-------HFVKDEKTRFGLALECG---N 656
Cdd:cd22938  301 YDmadEVLPMVRNAKrtrvahflekqgfkqqaLVGSSDIAYLFELALPEGALkiayqlaHFVKDEKKWFSLALECGskcN 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  657 IEIALEAAKALddkDCWDRLGQSALLQGNHQVVEMCYQRTKNF---DKLSFLYLITGnleKLKKMNKIAEIRK-DVSAQY 732
Cdd:cd22938  381 FELALEAAKAA---NDWEKLGLLALLQGNHQIVEMLAQRAENFgknNKAFFLYLITG---KLRKMMKLLIIRKrDMEAAF 454

                        490       500
                 ....*....|....*....|
gi 24655452  733 QGAL-LLGDVKERVNILKNC 751
Cdd:cd22938  455 LNATyLGDQVSERVRIWKEN 474
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 5-321 1.88e-72

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: 243.40  E-value: 1.88e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    5 FESKSARVKGLSFHPKRPWILVSLHSGVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWNYKQRR 84
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   85 CIFTLLAHLDYVRTVAFHHEYPWILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWDI 164
Cdd:cd00200   85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  165 SGLRkknvapgpgglddhlkghpgatdlfgqadavVKHVLEGHDRGVNWASFHPTLPLIVSGADDRLVKLWRMNeyKAWE 244
Cdd:cd00200  165 RTGK-------------------------------CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS--TGKC 211

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24655452  245 VDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWDMTKRQCLFTFRRDNERFWILTAHPTLN-LFAAGHDGGMVVFK 321
Cdd:cd00200  212 LGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKrLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
5-318 4.07e-56

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 200.52  E-value: 4.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    5 FESKSARVKGLSFHPKRPWILVSLHSGVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWNYKQRR 84
Cdd:COG2319   74 LLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   85 CIFTLLAHLDYVRTVAFHHEYPWILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWDI 164
Cdd:COG2319  154 LLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  165 SGLRKKNVAPGPGGL--------DDHL---KGHPGATDLFGQADAVVKHVLEGHDRGVNWASFHPTLPLIVSGADDRLVK 233
Cdd:COG2319  234 ATGKLLRTLTGHSGSvrsvafspDGRLlasGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVR 313

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  234 LWRMNEYKawEVDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWDMTKRQCLFTFRRDNERFWILTAHPTLNLFAAGH 313
Cdd:COG2319  314 LWDLATGK--LLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGS 391


                 ....*
gi 24655452  314 DGGMV 318
Cdd:COG2319  392 ADGTV 396
WD40 COG2319
WD40 repeat [General function prediction only];
2-282 4.03e-55

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 197.83  E-value: 4.03e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    2 LTNFESKSARVKGLSFHPKRPWILVSLHSGVIQLWDYRMHTLLEKFDEHDGPVRGVAFHqqmP---LFVSGGDDYKIKVW 78
Cdd:COG2319  113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFS---PdgkLLASGSDDGTVRLW 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   79 NYKQRRCIFTLLAHLDYVRTVAFHheyP---WILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASL 155
Cdd:COG2319  190 DLATGKLLRTLTGHTGAVRSVAFS---PdgkLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSA 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  156 DQTVRVWDISGLRKKNVAPGPGGLDDHLKGHPGATDLF-GQADAVVK----------HVLEGHDRGVNWASFHPTLPLIV 224
Cdd:COG2319  267 DGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLAsGSDDGTVRlwdlatgkllRTLTGHTGAVRSVAFSPDGKTLA 346

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24655452  225 SGADDRLVKLWRMNEykAWEVDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWDMT 282
Cdd:COG2319  347 SGSDDGTVRLWDLAT--GELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
9-318 3.75e-52

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 188.97  E-value: 3.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    9 SARVKGLSFHPKRPWILVSLHSGVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWNYKQRRCIFT 88
Cdd:COG2319   36 AAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRT 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   89 LLAHLDYVRTVAFHHEYPWILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWDISGlr 168
Cdd:COG2319  116 LTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT-- 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  169 kknvapgpGGLDDHLKGHPGA-TDL----------FGQADAVVK----------HVLEGHDRGVNWASFHPTLPLIVSGA 227
Cdd:COG2319  194 --------GKLLRTLTGHTGAvRSVafspdgkllaSGSADGTVRlwdlatgkllRTLTGHSGSVRSVAFSPDGRLLASGS 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  228 DDRLVKLWRMNEYKawEVDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWDMTKRQCLFTFRRDNERFWILTAHPTLN 307
Cdd:COG2319  266 ADGTVRLWDLATGE--LLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGK 343

                        330
                 ....*....|.
gi 24655452  308 LFAAGHDGGMV 318
Cdd:COG2319  344 TLASGSDDGTV 354
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 85-333 2.72e-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: 165.59  E-value: 2.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   85 CIFTLLAHLDYVRTVAFHHEYPWILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWDI 164
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  165 SGLRKKNVapgpgglddhLKGHPGA---------TDLF--GQADAVVK----------HVLEGHDRGVNWASFHPTLPLI 223
Cdd:cd00200   81 ETGECVRT----------LTGHTSYvssvafspdGRILssSSRDKTIKvwdvetgkclTTLRGHTDWVNSVAFSPDGTFV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  224 VSGADDRLVKLWRMNEYKawEVDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWDMTKRQCLFTFRRDNERFWILTAH 303
Cdd:cd00200  151 ASSSQDGTIKLWDLRTGK--CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFS 228

                        250       260       270
                 ....*....|....*....|....*....|.
gi 24655452  304 PTLNLFAAG-HDGGMVVFKLERERPAYAVHG 333
Cdd:cd00200  229 PDGYLLASGsEDGTIRVWDLRTGECVQTLSG 259
WD40 COG2319
WD40 repeat [General function prediction only];
16-335 8.46e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 158.92  E-value: 8.46e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   16 SFHPKRPWILVSLHSGVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWNYKQRRCIFTLLAHLDY 95
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   96 VRTVAFHHEYPWILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWDISGlrkknvapg 175
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT--------- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  176 pGGLDDHLKGHPGA-TDL-F---------GQADAVVK----------HVLEGHDRGVNWASFHPTLPLIVSGADDRLVKL 234
Cdd:COG2319  152 -GKLLRTLTGHSGAvTSVaFspdgkllasGSDDGTVRlwdlatgkllRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRL 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  235 WRMNEYKawEVDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWDMTKRQCLFTFRRDNERFWILTAHPTLNLFAAGHD 314
Cdd:COG2319  231 WDLATGK--LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSD 308

                        330       340
                 ....*....|....*....|..
gi 24655452  315 GGMV-VFKLERERPAYAVHGNI 335
Cdd:COG2319  309 DGTVrLWDLATGKLLRTLTGHT 330
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2-163 2.88e-39

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: 147.87  E-value: 2.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    2 LTNFESKSARVKGLSFHPKRPWILVSLHSGVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWNYK 81
Cdd:cd00200  128 LTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   82 QRRCIFTLLAHLDYVRTVAFHHEYPWILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRV 161
Cdd:cd00200  208 TGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287


                 ..
gi 24655452  162 WD 163
Cdd:cd00200  288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
2-166 1.47e-37

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 146.21  E-value: 1.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    2 LTNFESKSARVKGLSFHPKRPWILVSLHSGVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWNYK 81
Cdd:COG2319  239 LRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   82 QRRCIFTLLAHLDYVRTVAFHheyP---WILSASDDQTIRIWNWQSRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQT 158
Cdd:COG2319  319 TGKLLRTLTGHTGAVRSVAFS---PdgkTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395


                 ....*...
gi 24655452  159 VRVWDISG 166
Cdd:COG2319  396 VRLWDLAT 403
Coatomer_WDAD_beta-like cd22947
Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', ...
 424-772 1.89e-30

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: 126.81  E-value: 1.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  424 NRFAVLDRNQQLVI-KNFKNEVTKKLPTFCEEIFyagTGMLL-IRDPEFVTLY--EVQRLV---SVgsiklaKCRYVVWS 496
Cdd:cd22947   98 NYYAVRESSSSVKIfKNFKERKSFKPPFSAEGIF---GGALLgVRSSDFICFYdwETGKLVrriDV------EAKNVYWS 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  497 PDMSLVALLCKHSVTIcdrrLQY--------------------------LCTVQEncRVKSGAWdESGVFIYTTS-NHIK 549
Cdd:cd22947  169 ESGELVAIATDDSFYI----LRYnrdavaealesgeedeedgvedafevLHEISE--SVKSGLW-VGDCFIYTNSaNRLN 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  550 YAItnGDH-GIIRTLDLPIYLTRV--KGNQVFCLDREcrtrvLHIdpTEYKFKLALIQ------RK----YDEVL----- 611
Cdd:cd22947  242 YYV--GGEvVTIAHLDRPMYLLGYlpKDNRVYLIDKD-----LNV--VSYSLSLSVLEyqtavlRGdfeaADELLpsipe 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  612 -HMVRNARlvgqsiiaYLQQKGYPEVALHFVKDEKTRFGLALECGNIEIALEAAKALDDKDCWDRLGQSALLQGNHQVVE 690
Cdd:cd22947  313 dQRNKVAR--------FLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAE 384

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452  691 MCYQRTKNFDKLSFLYLITGNLEKLKKMNKIAEirkdVSAQY----QGALLLGDVKERVNILKNCGQLSLAYLTAATHGF 766
Cdd:cd22947  385 ECLKKAGDLSGLLLLYSSTGDKEGLEELAELAE----AAGKNniafLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCP 460


                 ....*.
gi 24655452  767 DELTES 772
Cdd:cd22947  461 SKVSEV 466
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 124-163 1.08e-09

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: 54.63  E-value: 1.08e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 24655452     124 SRNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWD 163
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
125-163 1.47e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 51.58  E-value: 1.47e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 24655452    125 RNCICVLTGHNHYVMCAQFHPTEDQIVSASLDQTVRVWD 163
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
83-121 5.24e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 5.24e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 24655452     83 RRCIFTLLAHLDYVRTVAFHHEYPWILSASDDQTIRIWN 121
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 82-121 1.17e-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: 48.85  E-value: 1.17e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 24655452      82 QRRCIFTLLAHLDYVRTVAFHHEYPWILSASDDQTIRIWN 121
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 31-165 1.30e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 56.25  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    31 GVIQLWDYRMHTLLEKFDEHDGPVRGVAFHQQMP-LFVSGGDDYKIKVWNYKQRRCIFTLLAHLDyVRTVAFHHEYPWIL 109
Cdd:PLN00181  555 GVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPtLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFPSESGRSL 633

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   110 S-ASDDQtiRIWNWQSRN---CICVLTGHNHYVMCAQFHPTEdQIVSASLDQTVRVWDIS 165
Cdd:PLN00181  634 AfGSADH--KVYYYDLRNpklPLCTMIGHSKTVSYVRFVDSS-TLVSSSTDNTLKLWDLS 690
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 42-79 2.34e-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: 45.38  E-value: 2.34e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 24655452      42 TLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWN 79
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 245-280 2.79e-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: 45.00  E-value: 2.79e-06
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 24655452     245 VDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWD 280
Cdd:smart00320    5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
245-280 5.10e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.26  E-value: 5.10e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 24655452    245 VDTCRGHYNNVSSVLFHPRQDLILSNGEDRSIRVWD 280
Cdd:pfam00400    4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 200-235 6.56e-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: 44.23  E-value: 6.56e-06
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 24655452     200 VKHVLEGHDRGVNWASFHPTLPLIVSGADDRLVKLW 235
Cdd:smart00320    4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
42-79 1.20e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.49  E-value: 1.20e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 24655452     42 TLLEKFDEHDGPVRGVAFHQQMPLFVSGGDDYKIKVWN 79
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
202-235 1.83e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.72  E-value: 1.83e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 24655452    202 HVLEGHDRGVNWASFHPTLPLIVSGADDRLVKLW 235
Cdd:pfam00400    5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00420 PTZ00420
coronin; Provisional
 75-169 1.06e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 43.40  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452    75 IKVWNYKQRRCIFTLLAHLDYVRTVAFHHEYPWIL-SASDDQTIRIW----NWQSRNCI----CVLTGHNHYVMCAQFHP 145
Cdd:PTZ00420   56 IRLENQMRKPPVIKLKGHTSSILDLQFNPCFSEILaSGSEDLTIRVWeiphNDESVKEIkdpqCILKGHKKKISIIDWNP 135

                          90       100
                  ....*....|....*....|....*
gi 24655452   146 TEDQIV-SASLDQTVRVWDISGLRK 169
Cdd:PTZ00420  136 MNYYIMcSSGFDSFVNIWDIENEKR 160
PTZ00421 PTZ00421
coronin; Provisional
 130-280 1.19e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 42.96  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655452   130 VLTGHNHYVMCAQFHPTEDQ-IVSASLDQTVRVWDI--SGLrKKNVApgpgglddhlkghpgatdlfgqaDAVVKhvLEG 206
Cdd:PTZ00421   70 ILLGQEGPIIDVAFNPFDPQkLFTASEDGTIMGWGIpeEGL-TQNIS-----------------------DPIVH--LQG 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24655452   207 HDRGVNWASFHPT-LPLIVSGADDRLVKLWRMNEYKAWEVDTCrgHYNNVSSVLFHPRQDLILSNGEDRSIRVWD 280
Cdd:PTZ00421  124 HTKKVGIVSFHPSaMNVLASAGADMVVNVWDVERGKAVEVIKC--HSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
 
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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