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Conserved domains on  [gi|2287254689|ref|NP_001397763|]
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coatomer subunit beta' isoform 2 [Homo sapiens]

Protein Classification

coatomer subunit beta'( domain architecture ID 17648131)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Coatomer_WDAD_beta-like cd22947
Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', ...
 275-749 0e+00

Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', also called beta'-coat protein; beta'-COP; p102, is a component of the coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunit. It is a heptameric complex that can polymerize into a cage to deform the membrane into a bud. This model corresponds to the WD-associated (WDAD) region found in coatomer subunits beta and beta' and is composed of a beta-propeller and an alpha-solenoid. The WD40 domain is found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly. It typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40. Between the GH and WD lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet. Each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade. The last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands allowing them to bind either stably or reversibly.


:

Pssm-ID: 438572  Cd Length: 475  Bit Score: 927.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 275 PAMSMDANGKIIWAKHSEVQQANLKAMGDAEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMAL 354
Cdd:cd22947     1 PAVSMDSSGKIIWAKHNEIQTANLKALDEEEDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 355 RNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWDNTELIRRIEI 434
Cdd:cd22947    81 RNKAFGSALEFVWSSDSNYYAVRESSSSVKIFKNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRIDV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 435 QPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRL 514
Cdd:cd22947   161 EAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSANRL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 515 NYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIISYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAH 594
Cdd:cd22947   241 NYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKVAR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 595 FLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLLLA 674
Cdd:cd22947   321 FLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLLLY 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2287254689 675 TASGNANMVNKLAEGAERDGKNNVAFMSYFLQGKVDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLS 749
Cdd:cd22947   401 SSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1-268 5.20e-63

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: 214.12  E-value: 5.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689   1 MLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHP 80
Cdd:cd00200    24 LATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  81 TQPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkdNNQF-ASASLDRTIKVWQLGSSSPNFTLEGHEKGV 159
Cdd:cd00200   104 DGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTGKCVATLTGHTGEV 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 160 NCIDYYSGGDKpyLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLN 239
Cdd:cd00200   181 NSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLS 258

                         250       260
                  ....*....|....*....|....*....
gi 2287254689 240 YGMERVWCVASLRGSNNVALGYDEGSIIV 268
Cdd:cd00200   259 GHTNSVTSLAWSPDGKRLASGSADGTIRI 287
 
Name Accession Description Interval E-value
Coatomer_WDAD_beta-like cd22947
Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', ...
 275-749 0e+00

Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', also called beta'-coat protein; beta'-COP; p102, is a component of the coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunit. It is a heptameric complex that can polymerize into a cage to deform the membrane into a bud. This model corresponds to the WD-associated (WDAD) region found in coatomer subunits beta and beta' and is composed of a beta-propeller and an alpha-solenoid. The WD40 domain is found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly. It typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40. Between the GH and WD lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet. Each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade. The last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands allowing them to bind either stably or reversibly.


Pssm-ID: 438572  Cd Length: 475  Bit Score: 927.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 275 PAMSMDANGKIIWAKHSEVQQANLKAMGDAEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMAL 354
Cdd:cd22947     1 PAVSMDSSGKIIWAKHNEIQTANLKALDEEEDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 355 RNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWDNTELIRRIEI 434
Cdd:cd22947    81 RNKAFGSALEFVWSSDSNYYAVRESSSSVKIFKNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRIDV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 435 QPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRL 514
Cdd:cd22947   161 EAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSANRL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 515 NYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIISYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAH 594
Cdd:cd22947   241 NYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKVAR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 595 FLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLLLA 674
Cdd:cd22947   321 FLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLLLY 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2287254689 675 TASGNANMVNKLAEGAERDGKNNVAFMSYFLQGKVDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLS 749
Cdd:cd22947   401 SSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 290-734 0e+00

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 596.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 290 HSEVQQANLKAMGDaeiKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAH 369
Cdd:pfam04053   1 ENEVRSYNIKGIEN---KDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 370 dSSEYAIRESNSIVKIFKNFKEK--KSFKPDFGAESIYG---GFLLGVRSVNGLAFYDWDNTELIRRIEIQP-KHIFWSD 443
Cdd:pfam04053  78 -RNRFAVLEKSGTVKIFKNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVSPvKYVIWSD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 444 SGELVCIATEESFFILKYLSEKVlaaqethegvtEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSvNRLNYYVGGEIV 523
Cdd:pfam04053 157 DGELVALLSKDTVYILNYNLEAV-----------EDGVEDAFEVLHEISERVKSGAWDGDVFIYTTS-NHLKYLVNGDSG 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 524 TIAHLDRTMYLLGYIPKDNRLYLGDKELNIISYSLLVSVLEYQTAVMRRDFSM------ADKVLPtiPKEQRTRVAHFLE 597
Cdd:pfam04053 225 IIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEEvlriirASNLLP--PKDEGQKIIRYLE 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 598 KQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLLLATAS 677
Cdd:pfam04053 303 KKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLST 382

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2287254689 678 GNANMVNKLAEGAERDGKNNVAFMSYFLQGKVDACLELLIRTGRLPEAAFLARTYLP 734
Cdd:pfam04053 383 GNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1-268 5.20e-63

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: 214.12  E-value: 5.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689   1 MLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHP 80
Cdd:cd00200    24 LATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  81 TQPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkdNNQF-ASASLDRTIKVWQLGSSSPNFTLEGHEKGV 159
Cdd:cd00200   104 DGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTGKCVATLTGHTGEV 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 160 NCIDYYSGGDKpyLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLN 239
Cdd:cd00200   181 NSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLS 258

                         250       260
                  ....*....|....*....|....*....
gi 2287254689 240 YGMERVWCVASLRGSNNVALGYDEGSIIV 268
Cdd:cd00200   259 GHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
1-268 1.80e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 185.89  E-value: 1.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689   1 MLASL-YNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVH 79
Cdd:COG2319   134 TLASGsADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFS 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  80 PTQPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGV 159
Cdd:COG2319   214 PDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATGELLRTLTGHSGGV 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 160 NCIDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLN 239
Cdd:COG2319   292 NSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLT 369

                         250       260
                  ....*....|....*....|....*....
gi 2287254689 240 YGMERVWCVASLRGSNNVALGYDEGSIIV 268
Cdd:COG2319   370 GHTGAVTSVAFSPDGRTLASGSADGTVRL 398
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 189-228 3.39e-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: 55.78  E-value: 3.39e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2287254689  189 NKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWH 228
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
190-227 1.69e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.89  E-value: 1.69e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2287254689 190 KTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIW 227
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00421 PTZ00421
coronin; Provisional
 116-226 5.37e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 52.97  E-value: 5.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 116 VMQIVINPKDNNQFASASLDRTIKVW-------QLGSSSPNFTLEGHEKGVNCIDYYSGGdKPYLISGADDRLVKIWDYQ 188
Cdd:PTZ00421   78 IIDVAFNPFDPQKLFTASEDGTIMGWgipeeglTQNISDPIVHLQGHTKKVGIVSFHPSA-MNVLASAGADMVVNVWDVE 156

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2287254689 189 NKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRI 226
Cdd:PTZ00421  157 RGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNI 194
 
Name Accession Description Interval E-value
Coatomer_WDAD_beta-like cd22947
Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', ...
 275-749 0e+00

Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', also called beta'-coat protein; beta'-COP; p102, is a component of the coatomer, which is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complexes are hetero-oligomers composed of at least an alpha, beta, beta', gamma, delta, epsilon and zeta subunit. It is a heptameric complex that can polymerize into a cage to deform the membrane into a bud. This model corresponds to the WD-associated (WDAD) region found in coatomer subunits beta and beta' and is composed of a beta-propeller and an alpha-solenoid. The WD40 domain is found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly. It typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40. Between the GH and WD lies a conserved core. It forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet. Each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade. The last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure. The residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands allowing them to bind either stably or reversibly.


Pssm-ID: 438572  Cd Length: 475  Bit Score: 927.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 275 PAMSMDANGKIIWAKHSEVQQANLKAMGDAEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMAL 354
Cdd:cd22947     1 PAVSMDSSGKIIWAKHNEIQTANLKALDEEEDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALAW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 355 RNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWDNTELIRRIEI 434
Cdd:cd22947    81 RNKAFGSALEFVWSSDSNYYAVRESSSSVKIFKNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRIDV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 435 QPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRL 514
Cdd:cd22947   161 EAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSANRL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 515 NYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIISYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAH 594
Cdd:cd22947   241 NYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKVAR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 595 FLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLLLA 674
Cdd:cd22947   321 FLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLLLY 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2287254689 675 TASGNANMVNKLAEGAERDGKNNVAFMSYFLQGKVDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLS 749
Cdd:cd22947   401 SSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
Coatomer_WDAD cd22938
Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds ...
 275-747 0e+00

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: 774.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 275 PAMSMDANGKIIWAKHSEvQQANLKAMGDAEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMAL 354
Cdd:cd22938     1 PAYSVDGNGKLHWVKHSE-QQADRFLRQLDFNSDGEKLVLVMKLRGSSKFPPQNMSHNPNGRFVLVCGDGEYDIYTAPAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 355 RNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSF--KPDFGAESIYGGFLLGVRSVNGLAFYDWDNTELIRRI 432
Cdd:cd22938    80 RNKSFGSAQTFVWVADSRFYALDRMHSSLKIKKNFKEITSKivPNCDEIFYAGTGNLLGVDSVDSITFFDWQNKRLLRRI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 433 EIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVN 512
Cdd:cd22938   160 KIKVKYVIWSDDGELVAILAKHSIVILNYLSEKVLAAQETHEGVTEDGIERAFDVLCEIHERVKSGAWVGDVFIYTTSSN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 513 RLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIISYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRV 592
Cdd:cd22938   240 RLNYAVGGGHGIIAHLDLPMYLLGYKGNDNNVYLLDRECRPRVYTIDPTVLEFQTALIRRKYDMADEVLPMVRNAKRTRV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 593 AHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLL 672
Cdd:cd22938   320 AHFLEKQGFKQQALVGSSDIAYLFELALPEGALKIAYQLAHFVKDEKKWFSLALECGSKCNFELALEAAKAANDWEKLGL 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2287254689 673 LATASGNANMVNKLAEGAERDGKNNVAFMSYFLQGKVDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWREN 747
Cdd:cd22938   400 LALLQGNHQIVEMLAQRAENFGKNNKAFFLYLITGKLRKMMKLLIIRKRDMEAAFLNATYLGDQVSERVRIWKEN 474
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 290-734 0e+00

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 596.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 290 HSEVQQANLKAMGDaeiKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAH 369
Cdd:pfam04053   1 ENEVRSYNIKGIEN---KDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 370 dSSEYAIRESNSIVKIFKNFKEK--KSFKPDFGAESIYG---GFLLGVRSVNGLAFYDWDNTELIRRIEIQP-KHIFWSD 443
Cdd:pfam04053  78 -RNRFAVLEKSGTVKIFKNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVSPvKYVIWSD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 444 SGELVCIATEESFFILKYLSEKVlaaqethegvtEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSvNRLNYYVGGEIV 523
Cdd:pfam04053 157 DGELVALLSKDTVYILNYNLEAV-----------EDGVEDAFEVLHEISERVKSGAWDGDVFIYTTS-NHLKYLVNGDSG 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 524 TIAHLDRTMYLLGYIPKDNRLYLGDKELNIISYSLLVSVLEYQTAVMRRDFSM------ADKVLPtiPKEQRTRVAHFLE 597
Cdd:pfam04053 225 IIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEEvlriirASNLLP--PKDEGQKIIRYLE 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 598 KQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLLLATAS 677
Cdd:pfam04053 303 KKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLST 382

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2287254689 678 GNANMVNKLAEGAERDGKNNVAFMSYFLQGKVDACLELLIRTGRLPEAAFLARTYLP 734
Cdd:pfam04053 383 GNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1-268 5.20e-63

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: 214.12  E-value: 5.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689   1 MLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHP 80
Cdd:cd00200    24 LATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  81 TQPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkdNNQF-ASASLDRTIKVWQLGSSSPNFTLEGHEKGV 159
Cdd:cd00200   104 DGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTGKCVATLTGHTGEV 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 160 NCIDYYSGGDKpyLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLN 239
Cdd:cd00200   181 NSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLS 258

                         250       260
                  ....*....|....*....|....*....
gi 2287254689 240 YGMERVWCVASLRGSNNVALGYDEGSIIV 268
Cdd:cd00200   259 GHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1-227 1.12e-57

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: 199.48  E-value: 1.12e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689   1 MLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHP 80
Cdd:cd00200    66 LASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  81 TQPFILTSSDDMLIKLWDwDKKWSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVN 160
Cdd:cd00200   146 DGTFVASSSQDGTIKLWD-LRTGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVN 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2287254689 161 CIDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIW 227
Cdd:cd00200   224 SVAFSPDGY--LLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 30-268 1.29e-55

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: 193.71  E-value: 1.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  30 PVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKwSCSQVF 109
Cdd:cd00200    11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG-ECVRTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 110 EGHTHYVMQIVINPkDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYysGGDKPYLISGADDRLVKIWDYQN 189
Cdd:cd00200    90 TGHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAF--SPDGTFVASSSQDGTIKLWDLRT 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2287254689 190 KTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIV 268
Cdd:cd00200   167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRV 245
WD40 COG2319
WD40 repeat [General function prediction only];
1-268 1.80e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 185.89  E-value: 1.80e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689   1 MLASL-YNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVH 79
Cdd:COG2319   134 TLASGsADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFS 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  80 PTQPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGV 159
Cdd:COG2319   214 PDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATGELLRTLTGHSGGV 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 160 NCIDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLN 239
Cdd:COG2319   292 NSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLT 369

                         250       260
                  ....*....|....*....|....*....
gi 2287254689 240 YGMERVWCVASLRGSNNVALGYDEGSIIV 268
Cdd:COG2319   370 GHTGAVTSVAFSPDGRTLASGSADGTVRL 398
WD40 COG2319
WD40 repeat [General function prediction only];
1-231 8.10e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 183.96  E-value: 8.10e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689   1 MLASL-YNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVH 79
Cdd:COG2319   176 LLASGsDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFS 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  80 PTQPFILTSSDDMLIKLWDWDKkWSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGV 159
Cdd:COG2319   256 PDGRLLASGSADGTVRLWDLAT-GELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAV 333

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2287254689 160 NCIDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSST 231
Cdd:COG2319   334 RSVAFSPDGK--TLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
2-268 9.39e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 178.18  E-value: 9.39e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689   2 LASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPT 81
Cdd:COG2319    52 AAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPD 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  82 QPFILTSSDDMLIKLWDWDKkWSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNC 161
Cdd:COG2319   132 GKTLASGSADGTVRLWDLAT-GKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 162 IDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYG 241
Cdd:COG2319   210 VAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGH 287

                         250       260
                  ....*....|....*....|....*..
gi 2287254689 242 MERVWCVASLRGSNNVALGYDEGSIIV 268
Cdd:COG2319   288 SGGVNSVAFSPDGKLLASGSDDGTVRL 314
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2-186 2.36e-41

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: 153.26  E-value: 2.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689   2 LASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPT 81
Cdd:cd00200   109 SSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPD 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  82 QPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNC 161
Cdd:cd00200   189 GEKLLSSSSDGTIKLWDLSTG-KCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTS 266

                         170       180
                  ....*....|....*....|....*
gi 2287254689 162 IDYYsgGDKPYLISGADDRLVKIWD 186
Cdd:cd00200   267 LAWS--PDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 105-268 3.90e-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: 144.01  E-value: 3.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 105 CSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSggDKPYLISGADDRLVKI 184
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 185 WDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEG 264
Cdd:cd00200    78 WDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157


                  ....
gi 2287254689 265 SIIV 268
Cdd:cd00200   158 TIKL 161
WD40 COG2319
WD40 repeat [General function prediction only];
12-268 1.02e-37

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 146.21  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  12 VWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDD 91
Cdd:COG2319    20 LLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASAD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  92 MLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYysGGDKP 171
Cdd:COG2319   100 GTVRLWDLATG-LLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAF--SPDGK 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 172 YLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASL 251
Cdd:COG2319   176 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFS 255

                         250
                  ....*....|....*..
gi 2287254689 252 RGSNNVALGYDEGSIIV 268
Cdd:COG2319   256 PDGRLLASGSADGTVRL 272
Coatomer_WDAD_alpha cd22948
Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called ...
 324-732 1.76e-17

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: 86.03  E-value: 1.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 324 IYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAI-----------RESNSIVKIFKNfKEK 392
Cdd:cd22948    44 QPPRSLSYNPAENAVLVTSDADGGSYELYTLPKDSSGAPEKPESKRGSGLSAVfvarnrfavldKSGTILIKNLEN-EVT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 393 KSFKPDFGAESIYG---GFLLgVRSVNGLAFYDWDNteliRRI--EIQ---PKHIFWSDSGELVCIATEESFFILkylse 464
Cdd:cd22948   123 KKIKPPPNVDKIFYagtGRVL-LRSEDKVILFDVQQ----KRVlaEVKvpkVKYVVWSKDMSHVALLSKHSITIA----- 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 465 kvlaaqethegvTEDgiedaFEVLGEIQEI--VKTGLWVGD-CFIYTSSvNRLNY-YVGGEIVTIAHLDRTMYLLGYipK 540
Cdd:cd22948   193 ------------TKK-----LEQLCSVHETirIKSGAWDESgVLIYTTL-NHIKYlLPNGDSGIIRTLDSPIYLTRV--K 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 541 DNRLYLGDKELNIisYSLLVSVLEYQT--AVMRRDFsmaDKVLPTIpkeqRTR------VAHFLEKQGFKQQALTVSTDP 612
Cdd:cd22948   253 GNTVYCLDREGKV--RVLEIDPTEYLFklALINKNY---DEVLRII----RSSklvgqsIIAYLQKKGYPEIALHFVKDP 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 613 EHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFGLAQECLHHAQDYGGLLLLATASGNANMVNKLAEGAER 692
Cdd:cd22948   324 KTRFNLALECGNLEVALEAAKELDDPECWERLAEEALRQGNHQIVEMAYQKTKNFDKLSFLYLITGNLEKLRKMLKIAEK 403

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 2287254689 693 DGKNNVAFMSYFLQGKVDACLELLIRTGRLPEAAFLARTY 732
Cdd:cd22948   404 RGDVMSRFQNALYLGDVEERVKILKEAGQLPLAYLTAKTH 443
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1-98 1.49e-15

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 78.15  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689   1 MLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHP 80
Cdd:cd00200   192 LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSP 271

                          90
                  ....*....|....*...
gi 2287254689  81 TQPFILTSSDDMLIKLWD 98
Cdd:cd00200   272 DGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 189-228 3.39e-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: 55.78  E-value: 3.39e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2287254689  189 NKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWH 228
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
190-227 1.69e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.89  E-value: 1.69e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2287254689 190 KTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIW 227
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 59-98 2.15e-08

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 50.77  E-value: 2.15e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2287254689   59 TLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWD 98
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
125-249 3.52e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.84  E-value: 3.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 125 DNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKpyLISGADDRLVKIWDYQNKTCVQTLEGHAQNVS 204
Cdd:COG2319     5 DGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGAR--LAAGAGDLTLLLLDAAAGALLATLLGHTAAVL 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2287254689 205 CASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVA 249
Cdd:COG2319    83 SVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVA 127
WD40 pfam00400
WD domain, G-beta repeat;
61-98 4.32e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 49.65  E-value: 4.32e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2287254689  61 ERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWD 98
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 102-141 1.83e-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: 48.08  E-value: 1.83e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2287254689  102 KWSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVW 141
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLW 39
PTZ00421 PTZ00421
coronin; Provisional
 116-226 5.37e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 52.97  E-value: 5.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 116 VMQIVINPKDNNQFASASLDRTIKVW-------QLGSSSPNFTLEGHEKGVNCIDYYSGGdKPYLISGADDRLVKIWDYQ 188
Cdd:PTZ00421   78 IIDVAFNPFDPQKLFTASEDGTIMGWgipeeglTQNISDPIVHLQGHTKKVGIVSFHPSA-MNVLASAGADMVVNVWDVE 156

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2287254689 189 NKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRI 226
Cdd:PTZ00421  157 RGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNI 194
WD40 pfam00400
WD domain, G-beta repeat;
146-186 1.20e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 1.20e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2287254689 146 SSPNFTLEGHEKGVNCIDYYSggDKPYLISGADDRLVKIWD 186
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSP--DGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
103-141 2.29e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.03  E-value: 2.29e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2287254689 103 WSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVW 141
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVW 38
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 127-211 2.58e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 51.24  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 127 NQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDyYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAqNVSCA 206
Cdd:PLN00181  546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSID-YSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKA-NICCV 623


                  ....*
gi 2287254689 207 SFHPE 211
Cdd:PLN00181  624 QFPSE 628
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 145-186 3.00e-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: 3.00e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2287254689  145 SSSPNFTLEGHEKGVNCIDYYSggDKPYLISGADDRLVKIWD 186
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP--DGKYLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
 109-190 4.36e-05

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 47.25  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 109 FEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSS--------SPNFTLEGHEKGVNCID-----YYsggdkpYLIS 175
Cdd:PTZ00420   70 LKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNdesvkeikDPQCILKGHKKKISIIDwnpmnYY------IMCS 143

                          90
                  ....*....|....*
gi 2287254689 176 GADDRLVKIWDYQNK 190
Cdd:PTZ00420  144 SGFDSFVNIWDIENE 158
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 40-230 1.44e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 45.46  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  40 KNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTS-SDDMLIKLWDWDKKWSCSQVfegHTHYVMQ 118
Cdd:PLN00181  545 KSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASgSDDGSVKLWSINQGVSIGTI---KTKANIC 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689 119 IVINPKDNNQ-FASASLDRTIKVWQLGSSS-PNFTLEGHEKGVNCIDYYsggDKPYLISGADDRLVKIWDYQ------NK 190
Cdd:PLN00181  622 CVQFPSESGRsLAFGSADHKVYYYDLRNPKlPLCTMIGHSKTVSYVRFV---DSSTLVSSSTDNTLKLWDLSmsisgiNE 698

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2287254689 191 TCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSS 230
Cdd:PLN00181  699 TPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKA 738
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
68-201 5.33e-04

Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 43.48  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  68 AHSDYIRCIAVHPTQPFILtSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQI--VIN-----PKDNNQFASASLDRTIKV 140
Cdd:COG5170   170 AHPYHINSISFNSDKETLL-SADDLRINLWNLEIIDGSFNIVDIKPHNMEELteVITsaefhPEMCNVFMYSSSKGEIKL 248

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2287254689 141 WQLGSSS----PNFTLEGHEKGVNcIDYYSG----------GDKPYLISGADDRLVKIWDYQN-KTCVQTLEGHAQ 201
Cdd:COG5170   249 NDLRQSAlcdnSKKLFELTIDGVD-VDFFEEivssisdfkfSDNGRYILSRDYLTVKIWDVNMaKNPIKTIPMHCD 323
PTZ00421 PTZ00421
coronin; Provisional
 83-200 1.11e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 42.57  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2287254689  83 PF----ILTSSDDMLIKLWDWDK---KWSCSQV---FEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTL 152
Cdd:PTZ00421   85 PFdpqkLFTASEDGTIMGWGIPEeglTQNISDPivhLQGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGKAVEVI 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2287254689 153 EGHEKGVNCIDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHA 200
Cdd:PTZ00421  165 KCHSDQITSLEWNLDGS--LLCTTSKDKKLNIIDPRDGTIVSSVEAHA 210
 
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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