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Conserved domains on  [gi|1907067170|ref|XP_036013272|]
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coatomer subunit alpha isoform X1 [Mus musculus]

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 ...
324-783 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: 840.25  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  324 PAYAVHGNMLHYVKDRFLRQLDFNSSK----DVAVMQLRSGSKFPVFNMSYNPAENAVLLCTRAsnlENSTYDLYTIPKD 399
Cdd:cd22948      1 PAFAVHGNSLYYVKDRKLRVYDFSSGSrvsvPVLSLRGRGGSNQPPRSLSYNPAENAVLVTSDA---DGGSYELYTLPKD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  400 ADSqNPDAPEGKRSSGLTAVWVARNRFAVLDRMHSLLIKNLKNEITKKIQVP-NCDEIFYAGTGNLLLRDADSITLFDVQ 478
Cdd:cd22948     78 SSG-APEKPESKRGSGLSAVFVARNRFAVLDKSGTILIKNLENEVTKKIKPPpNVDKIFYAGTGRVLLRSEDKVILFDVQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  479 QKRTLASVKISKVKYVIWSADMSHVALLAKHehscplpltAIVICNRKLDALCNIHENIRVKSGAWDESGVFIYTTSNHI 558
Cdd:cd22948    157 QKRVLAEVKVPKVKYVVWSKDMSHVALLSKH---------SITIATKKLEQLCSVHETIRIKSGAWDESGVLIYTTLNHI 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  559 KYAVTTGDHGIIRTLDLPIYVTRVKGNNVYCLDRECRPRVLTIDPTEFKFKLALINRKYDEVLHMVRNAKLVGQSIIAYL 638
Cdd:cd22948    228 KYLLPNGDSGIIRTLDSPIYLTRVKGNTVYCLDREGKVRVLEIDPTEYLFKLALINKNYDEVLRIIRSSKLVGQSIIAYL 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  639 QKKGYPEVALHFVKDEKTRFSLALECGNIEIALEAAKALDDKNCWEKLGEVALLQGNHQIVEMCYQRTKNFDKLSFLYLI 718
Cdd:cd22948    308 QKKGYPEIALHFVKDPKTRFNLALECGNLEVALEAAKELDDPECWERLAEEALRQGNHQIVEMAYQKTKNFDKLSFLYLI 387
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067170  719 TGNLEKLRKMMKIAEIRKDMSGHYQNALYLGDVSERVRILKNCGQKSLAYLSAATHGLDEEAESL 783
Cdd:cd22948    388 TGNLEKLRKMLKIAEKRGDVMSRFQNALYLGDVEERVKILKEAGQLPLAYLTAKTHGLEELAEEI 452
COPI_C pfam06957
Coatomer (COPI) alpha subunit C-terminus; This family represents the C-terminus (approximately ...
825-1227 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: 753.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  825 GFFEGSIASKGKGGALAADIDIDTVGTEGWGEDAELQLDEdgFVEAPEGLGEDVL----GKGQEEGGGWDVEeDLELPPE 900
Cdd:pfam06957    1 GFFEGALAAAGGGSAAAVDEDDDEAAGAGWGDDADLDLDE--ANGGIEDEDDDEEegedGGDDDEEGGWDVE-DLELPPE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  901 LDVPSGVSGsAEDGFFVPPTKGTSPTQIWCNNSQLPVDHILAGSFETAMRLLHDQVGVIQFGPYKQLFLQTYARGRTTYQ 980
Cdd:pfam06957   78 LDVGAAAGA-ARSGYFVAPTPGVPPSQIWTNNSQLAVDHAAAGSFETAMRLLHRQLGVVNFAPLKPLFLDAYAGSRTSLR 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  981 ALPCLPSMYSYPNRNWKDAGLKNGVPAVGLKLNDLIQRLQLCYQLTTVGKFEEAVEKFRSILLSVPLLVVDNKQEIAEAQ 1060
Cdd:pfam06957  157 GLPSLPSLPGYPERNWSEDGAKNGPPALVYKLSQLEERLQAAYKLTTEGKFSEALRKFRSILHSIPLLVVDSKQEVDEVQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170 1061 QLITICREYIVGLCMEIERKKLPKeTLDQQKRICEMAAYFTHSNLQPVHMILVLRTALNLFFKLKNFKTAATFARRLLEL 1140
Cdd:pfam06957  237 QLITICREYIVGLRMETKRKELPK-SLDDQKRQAELAAYFTHCNLQPVHLILTLRTAMNLFFKLKNFKTAASFARRLLEL 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170 1141 GPKPEVAQQTRKILSACEKNPTDACQLNYDMHNPFDICAASYRPIYRGKPVEKCPLSGACYSPEFKGQICRVTTVTEIGK 1220
Cdd:pfam06957  316 GPPPKVAQQARKVLQACEKNPTDAHQLNYDEHNPFVVCGATFVPIYRGKPDVKCPYCGASYVPEFKGQVCTVCQVAEIGK 395

                   ....*..
gi 1907067170 1221 DVIGLRI 1227
Cdd:pfam06957  396 DASGLRI 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
9-318 4.35e-73

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: 244.94  E-value: 4.35e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170    9 SARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYKLRRCLFT 88
Cdd:cd00200      9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   89 LLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRVWDISGLR 168
Cdd:cd00200     89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  169 kknlspgavesdvrgitgvdlfgttdavVKHVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIWRMNESKawEVDTCRGH 248
Cdd:cd00200    169 ----------------------------CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK--CLGTLRGH 218
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067170  249 YNNVSCAVFHPRQELILSNSEDKSIRVWDMSKRTGVQTFRRDHDRFWVLAAHPNLN-LFAAGHDGGMIVFK 318
Cdd:cd00200    219 ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKrLASGSADGTIRIWD 289
 
Name Accession Description Interval E-value
Coatomer_WDAD_alpha cd22948
Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called ...
324-783 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: 840.25  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  324 PAYAVHGNMLHYVKDRFLRQLDFNSSK----DVAVMQLRSGSKFPVFNMSYNPAENAVLLCTRAsnlENSTYDLYTIPKD 399
Cdd:cd22948      1 PAFAVHGNSLYYVKDRKLRVYDFSSGSrvsvPVLSLRGRGGSNQPPRSLSYNPAENAVLVTSDA---DGGSYELYTLPKD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  400 ADSqNPDAPEGKRSSGLTAVWVARNRFAVLDRMHSLLIKNLKNEITKKIQVP-NCDEIFYAGTGNLLLRDADSITLFDVQ 478
Cdd:cd22948     78 SSG-APEKPESKRGSGLSAVFVARNRFAVLDKSGTILIKNLENEVTKKIKPPpNVDKIFYAGTGRVLLRSEDKVILFDVQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  479 QKRTLASVKISKVKYVIWSADMSHVALLAKHehscplpltAIVICNRKLDALCNIHENIRVKSGAWDESGVFIYTTSNHI 558
Cdd:cd22948    157 QKRVLAEVKVPKVKYVVWSKDMSHVALLSKH---------SITIATKKLEQLCSVHETIRIKSGAWDESGVLIYTTLNHI 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  559 KYAVTTGDHGIIRTLDLPIYVTRVKGNNVYCLDRECRPRVLTIDPTEFKFKLALINRKYDEVLHMVRNAKLVGQSIIAYL 638
Cdd:cd22948    228 KYLLPNGDSGIIRTLDSPIYLTRVKGNTVYCLDREGKVRVLEIDPTEYLFKLALINKNYDEVLRIIRSSKLVGQSIIAYL 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  639 QKKGYPEVALHFVKDEKTRFSLALECGNIEIALEAAKALDDKNCWEKLGEVALLQGNHQIVEMCYQRTKNFDKLSFLYLI 718
Cdd:cd22948    308 QKKGYPEIALHFVKDPKTRFNLALECGNLEVALEAAKELDDPECWERLAEEALRQGNHQIVEMAYQKTKNFDKLSFLYLI 387
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067170  719 TGNLEKLRKMMKIAEIRKDMSGHYQNALYLGDVSERVRILKNCGQKSLAYLSAATHGLDEEAESL 783
Cdd:cd22948    388 TGNLEKLRKMLKIAEKRGDVMSRFQNALYLGDVEERVKILKEAGQLPLAYLTAKTHGLEELAEEI 452
COPI_C pfam06957
Coatomer (COPI) alpha subunit C-terminus; This family represents the C-terminus (approximately ...
825-1227 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: 753.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  825 GFFEGSIASKGKGGALAADIDIDTVGTEGWGEDAELQLDEdgFVEAPEGLGEDVL----GKGQEEGGGWDVEeDLELPPE 900
Cdd:pfam06957    1 GFFEGALAAAGGGSAAAVDEDDDEAAGAGWGDDADLDLDE--ANGGIEDEDDDEEegedGGDDDEEGGWDVE-DLELPPE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  901 LDVPSGVSGsAEDGFFVPPTKGTSPTQIWCNNSQLPVDHILAGSFETAMRLLHDQVGVIQFGPYKQLFLQTYARGRTTYQ 980
Cdd:pfam06957   78 LDVGAAAGA-ARSGYFVAPTPGVPPSQIWTNNSQLAVDHAAAGSFETAMRLLHRQLGVVNFAPLKPLFLDAYAGSRTSLR 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  981 ALPCLPSMYSYPNRNWKDAGLKNGVPAVGLKLNDLIQRLQLCYQLTTVGKFEEAVEKFRSILLSVPLLVVDNKQEIAEAQ 1060
Cdd:pfam06957  157 GLPSLPSLPGYPERNWSEDGAKNGPPALVYKLSQLEERLQAAYKLTTEGKFSEALRKFRSILHSIPLLVVDSKQEVDEVQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170 1061 QLITICREYIVGLCMEIERKKLPKeTLDQQKRICEMAAYFTHSNLQPVHMILVLRTALNLFFKLKNFKTAATFARRLLEL 1140
Cdd:pfam06957  237 QLITICREYIVGLRMETKRKELPK-SLDDQKRQAELAAYFTHCNLQPVHLILTLRTAMNLFFKLKNFKTAASFARRLLEL 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170 1141 GPKPEVAQQTRKILSACEKNPTDACQLNYDMHNPFDICAASYRPIYRGKPVEKCPLSGACYSPEFKGQICRVTTVTEIGK 1220
Cdd:pfam06957  316 GPPPKVAQQARKVLQACEKNPTDAHQLNYDEHNPFVVCGATFVPIYRGKPDVKCPYCGASYVPEFKGQVCTVCQVAEIGK 395

                   ....*..
gi 1907067170 1221 DVIGLRI 1227
Cdd:pfam06957  396 DASGLRI 402
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
338-776 0e+00

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 544.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  338 DRFLRQLDF----NSSKDVAVMQLRSGSKFPVF--NMSYNPAENAVLLCtrasnlENSTYDLYTIPkdadsqnpDAPEGK 411
Cdd:pfam04053    1 ENEVRSYNIkgieNKDGELLSLSLKELGSVEIYpqTLSHNPNGRFVLVC------GDGEYIIYTAL--------AWRNKA 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  412 RSSGLTAVWVARNRFAVLDRMHSLLI-KNLKNEITKKIQVP-NCDEIFYAGTGNLLLRDADS-ITLFDVQQKRTLASVKI 488
Cdd:pfam04053   67 YGKGLDFVWVSRNRFAVLEKSGTVKIfKNFKESVTKSIKLPySVDKIFGGGPGSLLGVKSEGsLSFYDWEQGKLVRRIDV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  489 SKVKYVIWSADMSHVALLAKHehscplpltAIVICNRKL--------DALCNIHE-NIRVKSGAWDESgVFIYTTSNHIK 559
Cdd:pfam04053  147 SPVKYVIWSDDGELVALLSKD---------TVYILNYNLeavedgveDAFEVLHEiSERVKSGAWDGD-VFIYTTSNHLK 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  560 YAVTtGDHGIIRTLDLPIYVTRVKG--NNVYCLDRECRPRVLTIDPTEFKFKLALINRKYDEVLHMVRNAKLV-----GQ 632
Cdd:pfam04053  217 YLVN-GDSGIIKTLDKTLYLLGYLGkeNRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEEVLRIIRASNLLppkdeGQ 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  633 SIIAYLQKKGYPEVALHFVKDEKTRFSLALECGNIEIALEAAKALDDKNCWEKLGEVALLQGNHQIVEMCYQRTKNFDKL 712
Cdd:pfam04053  296 KIIRYLEKKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKL 375
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067170  713 SFLYLITGNLEKLRKMMKIAEIRKDMSGHYQNALYLGDVSERVRILKNCGQKSLAYLSAATHGL 776
Cdd:pfam04053  376 LLLYLSTGNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
9-318 4.35e-73

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: 244.94  E-value: 4.35e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170    9 SARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYKLRRCLFT 88
Cdd:cd00200      9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   89 LLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRVWDISGLR 168
Cdd:cd00200     89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  169 kknlspgavesdvrgitgvdlfgttdavVKHVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIWRMNESKawEVDTCRGH 248
Cdd:cd00200    169 ----------------------------CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK--CLGTLRGH 218
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067170  249 YNNVSCAVFHPRQELILSNSEDKSIRVWDMSKRTGVQTFRRDHDRFWVLAAHPNLN-LFAAGHDGGMIVFK 318
Cdd:cd00200    219 ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKrLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
2-315 8.40e-56

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 199.75  E-value: 8.40e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170    2 LTKFETKSARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYK 81
Cdd:COG2319     71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   82 LRRCLFTLLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRV 161
Cdd:COG2319    151 TGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRL 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  162 WDISGLRKKNLSPGAvESDVRGI----------TG-----VDLFGTTDAVVKHVLEGHDRGVNWAAFHPTMPLIVSGADD 226
Cdd:COG2319    231 WDLATGKLLRTLTGH-SGSVRSVafspdgrllaSGsadgtVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDD 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  227 RQVKIWRMNESKawEVDTCRGHYNNVSCAVFHPRQELILSNSEDKSIRVWDMSKRTGVQTFRRDHDRFWVLAAHPNLNLF 306
Cdd:COG2319    310 GTVRLWDLATGK--LLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTL 387

                   ....*....
gi 1907067170  307 AAGHDGGMI 315
Cdd:COG2319    388 ASGSADGTV 396
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
124-163 9.52e-10

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: 55.01  E-value: 9.52e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1907067170   124 SRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRVWD 163
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
125-163 4.62e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.12  E-value: 4.62e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1907067170  125 RTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRVWD 163
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
24-189 6.13e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 60.49  E-value: 6.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   24 ILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQP-LFVSGGDDYKIKVWNYKLRRCLFTLLGHLDYIRTTFFH 102
Cdd:PLN00181   548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPtLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFPS 627
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  103 HEYPWILSASDDQTIRVWNWQS-RTCVCVLTGHNHYVMCAQFHPSEDLvVSASLDQTVRVWD----ISGLRKKNLSPGAV 177
Cdd:PLN00181   628 ESGRSLAFGSADHKVYYYDLRNpKLPLCTMIGHSKTVSYVRFVDSSTL-VSSSTDNTLKLWDlsmsISGINETPLHSFMG 706
                          170
                   ....*....|..
gi 1907067170  178 ESDVRGITGVDL 189
Cdd:PLN00181   707 HTNVKNFVGLSV 718
HOT cd08190
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ...
867-949 8.13e-03

Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.


Pssm-ID: 341469 [Multi-domain]  Cd Length: 412  Bit Score: 40.22  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  867 FVEAPEGLGEDVLGKGQEEGGGWDVEEDLELPPELDVPSGVSG---SAEDgffVPP-TKGTSPTQIWCNNSQLPVD-HIL 941
Cdd:cd08190    328 HLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSAlgySEDD---IPAlVEGTLPQQRLLKLNPRPVTeEDL 404

                   ....*...
gi 1907067170  942 AGSFETAM 949
Cdd:cd08190    405 EEIFEDAL 412
 
Name Accession Description Interval E-value
Coatomer_WDAD_alpha cd22948
Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called ...
324-783 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: 840.25  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  324 PAYAVHGNMLHYVKDRFLRQLDFNSSK----DVAVMQLRSGSKFPVFNMSYNPAENAVLLCTRAsnlENSTYDLYTIPKD 399
Cdd:cd22948      1 PAFAVHGNSLYYVKDRKLRVYDFSSGSrvsvPVLSLRGRGGSNQPPRSLSYNPAENAVLVTSDA---DGGSYELYTLPKD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  400 ADSqNPDAPEGKRSSGLTAVWVARNRFAVLDRMHSLLIKNLKNEITKKIQVP-NCDEIFYAGTGNLLLRDADSITLFDVQ 478
Cdd:cd22948     78 SSG-APEKPESKRGSGLSAVFVARNRFAVLDKSGTILIKNLENEVTKKIKPPpNVDKIFYAGTGRVLLRSEDKVILFDVQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  479 QKRTLASVKISKVKYVIWSADMSHVALLAKHehscplpltAIVICNRKLDALCNIHENIRVKSGAWDESGVFIYTTSNHI 558
Cdd:cd22948    157 QKRVLAEVKVPKVKYVVWSKDMSHVALLSKH---------SITIATKKLEQLCSVHETIRIKSGAWDESGVLIYTTLNHI 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  559 KYAVTTGDHGIIRTLDLPIYVTRVKGNNVYCLDRECRPRVLTIDPTEFKFKLALINRKYDEVLHMVRNAKLVGQSIIAYL 638
Cdd:cd22948    228 KYLLPNGDSGIIRTLDSPIYLTRVKGNTVYCLDREGKVRVLEIDPTEYLFKLALINKNYDEVLRIIRSSKLVGQSIIAYL 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  639 QKKGYPEVALHFVKDEKTRFSLALECGNIEIALEAAKALDDKNCWEKLGEVALLQGNHQIVEMCYQRTKNFDKLSFLYLI 718
Cdd:cd22948    308 QKKGYPEIALHFVKDPKTRFNLALECGNLEVALEAAKELDDPECWERLAEEALRQGNHQIVEMAYQKTKNFDKLSFLYLI 387
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907067170  719 TGNLEKLRKMMKIAEIRKDMSGHYQNALYLGDVSERVRILKNCGQKSLAYLSAATHGLDEEAESL 783
Cdd:cd22948    388 TGNLEKLRKMLKIAEKRGDVMSRFQNALYLGDVEERVKILKEAGQLPLAYLTAKTHGLEELAEEI 452
COPI_C pfam06957
Coatomer (COPI) alpha subunit C-terminus; This family represents the C-terminus (approximately ...
825-1227 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: 753.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  825 GFFEGSIASKGKGGALAADIDIDTVGTEGWGEDAELQLDEdgFVEAPEGLGEDVL----GKGQEEGGGWDVEeDLELPPE 900
Cdd:pfam06957    1 GFFEGALAAAGGGSAAAVDEDDDEAAGAGWGDDADLDLDE--ANGGIEDEDDDEEegedGGDDDEEGGWDVE-DLELPPE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  901 LDVPSGVSGsAEDGFFVPPTKGTSPTQIWCNNSQLPVDHILAGSFETAMRLLHDQVGVIQFGPYKQLFLQTYARGRTTYQ 980
Cdd:pfam06957   78 LDVGAAAGA-ARSGYFVAPTPGVPPSQIWTNNSQLAVDHAAAGSFETAMRLLHRQLGVVNFAPLKPLFLDAYAGSRTSLR 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  981 ALPCLPSMYSYPNRNWKDAGLKNGVPAVGLKLNDLIQRLQLCYQLTTVGKFEEAVEKFRSILLSVPLLVVDNKQEIAEAQ 1060
Cdd:pfam06957  157 GLPSLPSLPGYPERNWSEDGAKNGPPALVYKLSQLEERLQAAYKLTTEGKFSEALRKFRSILHSIPLLVVDSKQEVDEVQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170 1061 QLITICREYIVGLCMEIERKKLPKeTLDQQKRICEMAAYFTHSNLQPVHMILVLRTALNLFFKLKNFKTAATFARRLLEL 1140
Cdd:pfam06957  237 QLITICREYIVGLRMETKRKELPK-SLDDQKRQAELAAYFTHCNLQPVHLILTLRTAMNLFFKLKNFKTAASFARRLLEL 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170 1141 GPKPEVAQQTRKILSACEKNPTDACQLNYDMHNPFDICAASYRPIYRGKPVEKCPLSGACYSPEFKGQICRVTTVTEIGK 1220
Cdd:pfam06957  316 GPPPKVAQQARKVLQACEKNPTDAHQLNYDEHNPFVVCGATFVPIYRGKPDVKCPYCGASYVPEFKGQVCTVCQVAEIGK 395

                   ....*..
gi 1907067170 1221 DVIGLRI 1227
Cdd:pfam06957  396 DASGLRI 402
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
338-776 0e+00

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 544.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  338 DRFLRQLDF----NSSKDVAVMQLRSGSKFPVF--NMSYNPAENAVLLCtrasnlENSTYDLYTIPkdadsqnpDAPEGK 411
Cdd:pfam04053    1 ENEVRSYNIkgieNKDGELLSLSLKELGSVEIYpqTLSHNPNGRFVLVC------GDGEYIIYTAL--------AWRNKA 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  412 RSSGLTAVWVARNRFAVLDRMHSLLI-KNLKNEITKKIQVP-NCDEIFYAGTGNLLLRDADS-ITLFDVQQKRTLASVKI 488
Cdd:pfam04053   67 YGKGLDFVWVSRNRFAVLEKSGTVKIfKNFKESVTKSIKLPySVDKIFGGGPGSLLGVKSEGsLSFYDWEQGKLVRRIDV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  489 SKVKYVIWSADMSHVALLAKHehscplpltAIVICNRKL--------DALCNIHE-NIRVKSGAWDESgVFIYTTSNHIK 559
Cdd:pfam04053  147 SPVKYVIWSDDGELVALLSKD---------TVYILNYNLeavedgveDAFEVLHEiSERVKSGAWDGD-VFIYTTSNHLK 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  560 YAVTtGDHGIIRTLDLPIYVTRVKG--NNVYCLDRECRPRVLTIDPTEFKFKLALINRKYDEVLHMVRNAKLV-----GQ 632
Cdd:pfam04053  217 YLVN-GDSGIIKTLDKTLYLLGYLGkeNRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEEVLRIIRASNLLppkdeGQ 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  633 SIIAYLQKKGYPEVALHFVKDEKTRFSLALECGNIEIALEAAKALDDKNCWEKLGEVALLQGNHQIVEMCYQRTKNFDKL 712
Cdd:pfam04053  296 KIIRYLEKKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKL 375
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067170  713 SFLYLITGNLEKLRKMMKIAEIRKDMSGHYQNALYLGDVSERVRILKNCGQKSLAYLSAATHGL 776
Cdd:pfam04053  376 LLLYLSTGNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
Coatomer_WDAD cd22938
Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds ...
324-761 6.05e-175

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: 524.95  E-value: 6.05e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  324 PAYAVHGN-MLHYVK------DRFLRQLDFNS--SKDVAVMQLRSGSKFPVFNMSYNPAENAVLLCTRAsnlensTYDLY 394
Cdd:cd22938      1 PAYSVDGNgKLHWVKhseqqaDRFLRQLDFNSdgEKLVLVMKLRGSSKFPPQNMSHNPNGRFVLVCGDG------EYDIY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  395 TipkdadsqnpdAPEGKRSSG---LTAVWVARNRFAVLDRMH-SLLIKNLKNEITKKIqVPNCDEIFYAGTGNLLLRDA- 469
Cdd:cd22938     75 T-----------APAGRNKSFgsaQTFVWVADSRFYALDRMHsSLKIKKNFKEITSKI-VPNCDEIFYAGTGNLLGVDSv 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  470 DSITLFDVQQKRTLASVKIsKVKYVIWSADMSHVALLAKHehscplpltAIVICN----------------------RKL 527
Cdd:cd22938    143 DSITFFDWQNKRLLRRIKI-KVKYVIWSDDGELVAILAKH---------SIVILNylsekvlaaqethegvtedgieRAF 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  528 DALCNIHEniRVKSGAWDEsGVFIYTT-SNHIKYAVTTGdHGIIRTLDLPIYVTRVKG--NNVYCLDRECRPRVLTIDPT 604
Cdd:cd22938    213 DVLCEIHE--RVKSGAWVG-DVFIYTTsSNRLNYAVGGG-HGIIAHLDLPMYLLGYKGndNNVYLLDRECRPRVYTIDPT 288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  605 EFKFKLALINRKYD---EVLHMVRNAK-----------------LVGQSIIAYLQKKGYPEVAL-------HFVKDEKTR 657
Cdd:cd22938    289 VLEFQTALIRRKYDmadEVLPMVRNAKrtrvahflekqgfkqqaLVGSSDIAYLFELALPEGALkiayqlaHFVKDEKKW 368
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  658 FSLALECG---NIEIALEAAKALddkNCWEKLGEVALLQGNHQIVEMCYQRTKNF---DKLSFLYLITGnleKLRKMMKI 731
Cdd:cd22938    369 FSLALECGskcNFELALEAAKAA---NDWEKLGLLALLQGNHQIVEMLAQRAENFgknNKAFFLYLITG---KLRKMMKL 442
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1907067170  732 AEIRK-DMSGHYQNALYLGD-VSERVRILKNC 761
Cdd:cd22938    443 LIIRKrDMEAAFLNATYLGDqVSERVRIWKEN 474
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
9-318 4.35e-73

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: 244.94  E-value: 4.35e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170    9 SARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYKLRRCLFT 88
Cdd:cd00200      9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   89 LLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRVWDISGLR 168
Cdd:cd00200     89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  169 kknlspgavesdvrgitgvdlfgttdavVKHVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIWRMNESKawEVDTCRGH 248
Cdd:cd00200    169 ----------------------------CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGK--CLGTLRGH 218
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907067170  249 YNNVSCAVFHPRQELILSNSEDKSIRVWDMSKRTGVQTFRRDHDRFWVLAAHPNLN-LFAAGHDGGMIVFK 318
Cdd:cd00200    219 ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKrLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
2-315 8.40e-56

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 199.75  E-value: 8.40e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170    2 LTKFETKSARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYK 81
Cdd:COG2319     71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   82 LRRCLFTLLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRV 161
Cdd:COG2319    151 TGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRL 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  162 WDISGLRKKNLSPGAvESDVRGI----------TG-----VDLFGTTDAVVKHVLEGHDRGVNWAAFHPTMPLIVSGADD 226
Cdd:COG2319    231 WDLATGKLLRTLTGH-SGSVRSVafspdgrllaSGsadgtVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDD 309
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  227 RQVKIWRMNESKawEVDTCRGHYNNVSCAVFHPRQELILSNSEDKSIRVWDMSKRTGVQTFRRDHDRFWVLAAHPNLNLF 306
Cdd:COG2319    310 GTVRLWDLATGK--LLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTL 387

                   ....*....
gi 1907067170  307 AAGHDGGMI 315
Cdd:COG2319    388 ASGSADGTV 396
WD40 COG2319
WD40 repeat [General function prediction only];
2-279 2.20e-52

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 189.74  E-value: 2.20e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170    2 LTKFETKSARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYK 81
Cdd:COG2319    155 LRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   82 LRRCLFTLLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRV 161
Cdd:COG2319    235 TGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRL 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  162 WDISGLRkknlspgavesdvrgitgvdlfgttdavVKHVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIWRMNESKawE 241
Cdd:COG2319    315 WDLATGK----------------------------LLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGE--L 364
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1907067170  242 VDTCRGHYNNVSCAVFHPRQELILSNSEDKSIRVWDMS 279
Cdd:COG2319    365 LRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
16-331 3.66e-41

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 157.00  E-value: 3.66e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   16 SFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYKLRRCLFTLLGHLDY 95
Cdd:COG2319      1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   96 IRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRVWDISGLRKKNLSPG 175
Cdd:COG2319     81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  176 AvESDVRGIT----GVDLF-GTTDAVVK----------HVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIWRMNESKaw 240
Cdd:COG2319    161 H-SGAVTSVAfspdGKLLAsGSDDGTVRlwdlatgkllRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK-- 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  241 EVDTCRGHYNNVSCAVFHPRQELILSNSEDKSIRVWDMSKRTGVQTFRRDHDRFWVLAAHPNLNLFAAGHDGGMI-VFKL 319
Cdd:COG2319    238 LLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVrLWDL 317
                          330
                   ....*....|..
gi 1907067170  320 ERERPAYAVHGN 331
Cdd:COG2319    318 ATGKLLRTLTGH 329
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
2-163 3.06e-38

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 145.17  E-value: 3.06e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170    2 LTKFETKSARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYK 81
Cdd:cd00200    128 LTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   82 LRRCLFTLLGHLDYIRTTFFHHEYPWILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRV 161
Cdd:cd00200    208 TGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287

                   ..
gi 1907067170  162 WD 163
Cdd:cd00200    288 WD 289
WD40 COG2319
WD40 repeat [General function prediction only];
2-166 2.25e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 136.96  E-value: 2.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170    2 LTKFETKSARVKGLSFHPKRPWILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWNYK 81
Cdd:COG2319    239 LRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   82 LRRCLFTLLGHLDYIRTTFFHheyP---WILSASDDQTIRVWNWQSRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQT 158
Cdd:COG2319    319 TGKLLRTLTGHTGAVRSVAFS---PdgkTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395

                   ....*...
gi 1907067170  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', ...
414-784 2.50e-22

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: 102.16  E-value: 2.50e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  414 SGLTAVWVAR-NRFAVLDRMHSLLI-KNLKNeiTKKIQVP-NCDEIFyagTGNLL-LRDADSITLFDVQqkrTLASV-KI 488
Cdd:cd22947     87 SALEFVWSSDsNYYAVRESSSSVKIfKNFKE--RKSFKPPfSAEGIF---GGALLgVRSSDFICFYDWE---TGKLVrRI 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  489 S-KVKYVIWSADMSHVALlakhehSCPlplTAIVICNRKLDA----------------------LCNIHEniRVKSGAWd 545
Cdd:cd22947    159 DvEAKNVYWSESGELVAI------ATD---DSFYILRYNRDAvaealesgeedeedgvedafevLHEISE--SVKSGLW- 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  546 ESGVFIYTTS-NHIKYAVttGDH-GIIRTLDLPIYVTRV--KGNNVYCLDREcrprvLTIdpTEFKFKLALIN------R 615
Cdd:cd22947    227 VGDCFIYTNSaNRLNYYV--GGEvVTIAHLDRPMYLLGYlpKDNRVYLIDKD-----LNV--VSYSLSLSVLEyqtavlR 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  616 K----YDEVL------HMVRNAKlvgqsiiaYLQKKGYPEVALHFVKDEKTRFSLALECGNIEIALEAAKALDDKNCWEK 685
Cdd:cd22947    298 GdfeaADELLpsipedQRNKVAR--------FLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQ 369
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  686 LGEVALLQGNHQIVEMCYQRTKNFDKLSFLYLITGNLEKLRKMMKIAEirkdMSGHYQ---NALYL-GDVSERVRILKNC 761
Cdd:cd22947    370 LGDLALSKGDFDLAEECLKKAGDLSGLLLLYSSTGDKEGLEELAELAE----AAGKNNiafLAYFLlGDLDKCVDLLIKT 445
                          410       420
                   ....*....|....*....|...
gi 1907067170  762 GQKSLAYLSAATHGLDEEAESLK 784
Cdd:cd22947    446 GRLPEAAFFARTYCPSKVSEVVK 468
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
124-163 9.52e-10

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: 55.01  E-value: 9.52e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1907067170   124 SRTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRVWD 163
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
125-163 4.62e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.12  E-value: 4.62e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1907067170  125 RTCVCVLTGHNHYVMCAQFHPSEDLVVSASLDQTVRVWD 163
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
24-189 6.13e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 60.49  E-value: 6.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170   24 ILTSLHNGVIQLWDYRMCTLIDKFDEHDGPVRGIDFHKQQP-LFVSGGDDYKIKVWNYKLRRCLFTLLGHLDYIRTTFFH 102
Cdd:PLN00181   548 VASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPtLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQFPS 627
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  103 HEYPWILSASDDQTIRVWNWQS-RTCVCVLTGHNHYVMCAQFHPSEDLvVSASLDQTVRVWD----ISGLRKKNLSPGAV 177
Cdd:PLN00181   628 ESGRSLAFGSADHKVYYYDLRNpKLPLCTMIGHSKTVSYVRFVDSSTL-VSSSTDNTLKLWDlsmsISGINETPLHSFMG 706
                          170
                   ....*....|..
gi 1907067170  178 ESDVRGITGVDL 189
Cdd:PLN00181   707 HTNVKNFVGLSV 718
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
197-232 1.06e-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: 46.15  E-value: 1.06e-06
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1907067170   197 VKHVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIW 232
Cdd:smart00320    4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
242-277 1.63e-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: 45.77  E-value: 1.63e-06
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1907067170   242 VDTCRGHYNNVSCAVFHPRQELILSNSEDKSIRVWD 277
Cdd:smart00320    5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
83-121 2.97e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.03  E-value: 2.97e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1907067170   83 RRCLFTLLGHLDYIRTTFFHHEYPWILSASDDQTIRVWN 121
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
199-232 3.44e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.03  E-value: 3.44e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907067170  199 HVLEGHDRGVNWAAFHPTMPLIVSGADDRQVKIW 232
Cdd:pfam00400    5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
42-79 3.97e-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: 44.61  E-value: 3.97e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1907067170    42 TLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWN 79
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
242-277 4.62e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 4.62e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1907067170  242 VDTCRGHYNNVSCAVFHPRQELILSNSEDKSIRVWD 277
Cdd:pfam00400    4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
83-121 6.30e-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: 6.30e-06
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1907067170    83 RRCLFTLLGHLDYIRTTFFHHEYPWILSASDDQTIRVWN 121
Cdd:smart00320    2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
42-79 1.49e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.10  E-value: 1.49e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1907067170   42 TLIDKFDEHDGPVRGIDFHKQQPLFVSGGDDYKIKVWN 79
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
130-277 1.52e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 45.65  E-value: 1.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  130 VLTGHNHYVMCAQFHPSEDL-VVSASLDQTVRVWDI--SGLrKKNLSPGAVEsdvrgitgvdlfgttdavvkhvLEGHDR 206
Cdd:PTZ00421    70 ILLGQEGPIIDVAFNPFDPQkLFTASEDGTIMGWGIpeEGL-TQNISDPIVH----------------------LQGHTK 126
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907067170  207 GVNWAAFHPT-MPLIVSGADDRQVKIWRMNESKAWEVDTCrgHYNNVSCAVFHPRQELILSNSEDKSIRVWD 277
Cdd:PTZ00421   127 KVGIVSFHPSaMNVLASAGADMVVNVWDVERGKAVEVIKC--HSDQITSLEWNLDGSLLCTTSKDKKLNIID 196
HOT cd08190
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ...
867-949 8.13e-03

Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.


Pssm-ID: 341469 [Multi-domain]  Cd Length: 412  Bit Score: 40.22  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067170  867 FVEAPEGLGEDVLGKGQEEGGGWDVEEDLELPPELDVPSGVSG---SAEDgffVPP-TKGTSPTQIWCNNSQLPVD-HIL 941
Cdd:cd08190    328 HLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSAlgySEDD---IPAlVEGTLPQQRLLKLNPRPVTeEDL 404

                   ....*...
gi 1907067170  942 AGSFETAM 949
Cdd:cd08190    405 EEIFEDAL 412
 
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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