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Conserved domains on  [gi|1443060845|ref|XP_025879079|]
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putative coatomer subunit beta'-3 isoform X1 [Oryza sativa Japonica Group]

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', ...
 341-815 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: 824.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 341 PVASMDSSGKIIWSKHNEIQTVNIKTIGADnEIADGERLPLVVKELGTCDLYPQSLRHNPNGRFVVVCGDGEYIIYTALA 420
Cdd:cd22947     1 PAVSMDSSGKIIWAKHNEIQTANLKALDEE-EDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 421 WRNRSFGSALEFVWSLDG-EYAVRESTSRIKIYsKNFQERKSIRPPFSAERIFGGVLLAMCTNDFICFHDWAEGRMIRRI 499
Cdd:cd22947    80 WRNKAFGSALEFVWSSDSnYYAVRESSSSVKIF-KNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 500 DVNVKNLYWADSGDLVTIASDTSFYILKYNRDVVSSHLDGGGSVGEEGVEDAFELLHEINERIRTGLWVGDCFIYNNSSS 579
Cdd:cd22947   159 DVEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSAN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 580 RLNYCVGGEVTTLFHLDRQMYLLGYLANQSRVYLIDKQFNVVGYTLLLTMIEYKTLVMRGDFDRANALLPSIPKEQHDSV 659
Cdd:cd22947   239 RLNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 660 ARFLESRGMLEEALEIATDSNYRFDLAVQLGRLEVAKAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAMDLSGLLL 739
Cdd:cd22947   319 ARFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLL 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443060845 740 LYSSLGDAEGLTKLTSMAKEQGKNNVAFLCFFMLGKLEECLQLLIESNRIPEAALMSRSYLPSKVPEIVTLWKKDL 815
Cdd:cd22947   399 LYSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDL 474
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 57-334 1.29e-65

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


:

Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 222.21  E-value: 1.29e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  57 SVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADDMFIRVYNYNTMDKVKVFEAHT 136
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 137 DYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGwMCTQIFEGHSHYVMQVTFNPkdTNTF-ASASLDRTVKVWSLGSPDPN 215
Cdd:cd00200    94 SYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTGKCV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 216 FTLDGHSKGVNCVDYFTGGDRpyLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLWHS 295
Cdd:cd00200   171 ATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL 248

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1443060845 296 TTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMI 334
Cdd:cd00200   249 RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 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', ...
 341-815 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: 824.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 341 PVASMDSSGKIIWSKHNEIQTVNIKTIGADnEIADGERLPLVVKELGTCDLYPQSLRHNPNGRFVVVCGDGEYIIYTALA 420
Cdd:cd22947     1 PAVSMDSSGKIIWAKHNEIQTANLKALDEE-EDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 421 WRNRSFGSALEFVWSLDG-EYAVRESTSRIKIYsKNFQERKSIRPPFSAERIFGGVLLAMCTNDFICFHDWAEGRMIRRI 499
Cdd:cd22947    80 WRNKAFGSALEFVWSSDSnYYAVRESSSSVKIF-KNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 500 DVNVKNLYWADSGDLVTIASDTSFYILKYNRDVVSSHLDGGGSVGEEGVEDAFELLHEINERIRTGLWVGDCFIYNNSSS 579
Cdd:cd22947   159 DVEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSAN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 580 RLNYCVGGEVTTLFHLDRQMYLLGYLANQSRVYLIDKQFNVVGYTLLLTMIEYKTLVMRGDFDRANALLPSIPKEQHDSV 659
Cdd:cd22947   239 RLNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 660 ARFLESRGMLEEALEIATDSNYRFDLAVQLGRLEVAKAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAMDLSGLLL 739
Cdd:cd22947   319 ARFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLL 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443060845 740 LYSSLGDAEGLTKLTSMAKEQGKNNVAFLCFFMLGKLEECLQLLIESNRIPEAALMSRSYLPSKVPEIVTLWKKDL 815
Cdd:cd22947   399 LYSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDL 474
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 356-801 2.23e-177

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 521.41  E-value: 2.23e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 356 HNEIQTVNIKTigadNEIADGERLPLVVKELGTCDLYPQSLRHNPNGRFVVVCGDGEYIIYTALAWRNRSFGSALEFVWS 435
Cdd:pfam04053   1 ENEVRSYNIKG----IENKDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 436 LDGEYAVRESTSRIKIYsKNFQER--KSIRPPFSAERIFG---GVLLAMCTNDFICFHDWAEGRMIRRIDV-NVKNLYWA 509
Cdd:pfam04053  77 SRNRFAVLEKSGTVKIF-KNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVsPVKYVIWS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 510 DSGDLVTIASDTSFYILKYNRDVVSSHLDgggsvgeegveDAFELLHEINERIRTGLWVGDCFIYNNSSsRLNYCVGGEV 589
Cdd:pfam04053 156 DDGELVALLSKDTVYILNYNLEAVEDGVE-----------DAFEVLHEISERVKSGAWDGDVFIYTTSN-HLKYLVNGDS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 590 TTLFHLDRQMYLLGYLANQSRVYLIDKQFNVVGYTLLLTMIEYKTLVMRGDFD------RANALLPsiPKEQHDSVARFL 663
Cdd:pfam04053 224 GIIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEevlriiRASNLLP--PKDEGQKIIRYL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 664 ESRGMLEEALEIATDSNYRFDLAVQLGRLEVAKAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAMDLSGLLLLYSS 743
Cdd:pfam04053 302 EKKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLS 381

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1443060845 744 LGDAEGLTKLTSMAKEQGKNNVAFLCFFMLGKLEECLQLLIESNRIPEAALMSRSYLP 801
Cdd:pfam04053 382 TGNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 57-334 1.29e-65

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 222.21  E-value: 1.29e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  57 SVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADDMFIRVYNYNTMDKVKVFEAHT 136
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 137 DYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGwMCTQIFEGHSHYVMQVTFNPkdTNTF-ASASLDRTVKVWSLGSPDPN 215
Cdd:cd00200    94 SYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTGKCV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 216 FTLDGHSKGVNCVDYFTGGDRpyLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLWHS 295
Cdd:cd00200   171 ATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL 248

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1443060845 296 TTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMI 334
Cdd:cd00200   249 RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
46-334 2.04e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 209.00  E-value: 2.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  46 RKLAQRSERAKSVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADDMFIRVYNYNT 125
Cdd:COG2319   114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 126 MDKVKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGWmCTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTVK 205
Cdd:COG2319   194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK-LLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVR 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 206 VWSLGSPDPNFTLDGHSKGVNCVDyFTGgDRPYLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGS 285
Cdd:COG2319   272 LWDLATGELLRTLTGHSGGVNSVA-FSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGS 349

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1443060845 286 EDGTVRLWHSTTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMI 334
Cdd:COG2319   350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 255-294 4.02e-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: 4.02e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1443060845  255 TKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLWH 294
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
256-293 4.66e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 52.73  E-value: 4.66e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1443060845 256 KSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLW 293
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00421 PTZ00421
coronin; Provisional
 174-292 2.13e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.88  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 174 IFEGHSHYVMQVTFNPKDTNTFASASLDRTVKVWSL-------GSPDPNFTLDGHSKGVNCVDyFTGGDRPYLITGSDDQ 246
Cdd:PTZ00421   70 ILLGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIpeegltqNISDPIVHLQGHTKKVGIVS-FHPSAMNVLASAGADM 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1443060845 247 TAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRL 292
Cdd:PTZ00421  149 VVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNI 194
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 633-732 3.48e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 41.72  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 633 KTLVMRGDFDRANALLPSIPKEQHDSV------ARFLESRGMLEEALEIA--------TDSNYRFDLAV---QLGRLEVA 695
Cdd:COG4783    12 QALLLAGDYDEAEALLEKALELDPDNPeafallGEILLQLGDLDEAIVLLhealeldpDEPEARLNLGLallKAGDYDEA 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1443060845 696 -----KAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAM 732
Cdd:COG4783    92 lalleKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKAL 133
 
Name Accession Description Interval E-value
Coatomer_WDAD_beta-like cd22947
Coatomer WD Associated Region from Coatomer Subunit Beta and Beta'; Coatomer subunit beta', ...
 341-815 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: 824.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 341 PVASMDSSGKIIWSKHNEIQTVNIKTIGADnEIADGERLPLVVKELGTCDLYPQSLRHNPNGRFVVVCGDGEYIIYTALA 420
Cdd:cd22947     1 PAVSMDSSGKIIWAKHNEIQTANLKALDEE-EDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 421 WRNRSFGSALEFVWSLDG-EYAVRESTSRIKIYsKNFQERKSIRPPFSAERIFGGVLLAMCTNDFICFHDWAEGRMIRRI 499
Cdd:cd22947    80 WRNKAFGSALEFVWSSDSnYYAVRESSSSVKIF-KNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 500 DVNVKNLYWADSGDLVTIASDTSFYILKYNRDVVSSHLDGGGSVGEEGVEDAFELLHEINERIRTGLWVGDCFIYNNSSS 579
Cdd:cd22947   159 DVEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSAN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 580 RLNYCVGGEVTTLFHLDRQMYLLGYLANQSRVYLIDKQFNVVGYTLLLTMIEYKTLVMRGDFDRANALLPSIPKEQHDSV 659
Cdd:cd22947   239 RLNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 660 ARFLESRGMLEEALEIATDSNYRFDLAVQLGRLEVAKAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAMDLSGLLL 739
Cdd:cd22947   319 ARFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLL 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443060845 740 LYSSLGDAEGLTKLTSMAKEQGKNNVAFLCFFMLGKLEECLQLLIESNRIPEAALMSRSYLPSKVPEIVTLWKKDL 815
Cdd:cd22947   399 LYSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDL 474
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 356-801 2.23e-177

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 521.41  E-value: 2.23e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 356 HNEIQTVNIKTigadNEIADGERLPLVVKELGTCDLYPQSLRHNPNGRFVVVCGDGEYIIYTALAWRNRSFGSALEFVWS 435
Cdd:pfam04053   1 ENEVRSYNIKG----IENKDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 436 LDGEYAVRESTSRIKIYsKNFQER--KSIRPPFSAERIFG---GVLLAMCTNDFICFHDWAEGRMIRRIDV-NVKNLYWA 509
Cdd:pfam04053  77 SRNRFAVLEKSGTVKIF-KNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVsPVKYVIWS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 510 DSGDLVTIASDTSFYILKYNRDVVSSHLDgggsvgeegveDAFELLHEINERIRTGLWVGDCFIYNNSSsRLNYCVGGEV 589
Cdd:pfam04053 156 DDGELVALLSKDTVYILNYNLEAVEDGVE-----------DAFEVLHEISERVKSGAWDGDVFIYTTSN-HLKYLVNGDS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 590 TTLFHLDRQMYLLGYLANQSRVYLIDKQFNVVGYTLLLTMIEYKTLVMRGDFD------RANALLPsiPKEQHDSVARFL 663
Cdd:pfam04053 224 GIIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEevlriiRASNLLP--PKDEGQKIIRYL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 664 ESRGMLEEALEIATDSNYRFDLAVQLGRLEVAKAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAMDLSGLLLLYSS 743
Cdd:pfam04053 302 EKKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLS 381

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1443060845 744 LGDAEGLTKLTSMAKEQGKNNVAFLCFFMLGKLEECLQLLIESNRIPEAALMSRSYLP 801
Cdd:pfam04053 382 TGNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
Coatomer_WDAD cd22938
Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds ...
 341-812 1.52e-165

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: 492.20  E-value: 1.52e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 341 PVASMDSSGKIIWSKHNEIQTVNIKTigADNEIADGERLPLVVKELGTCDLYPQSLRHNPNGRFVVVCGDGEYIIYTALA 420
Cdd:cd22938     1 PAYSVDGNGKLHWVKHSEQQADRFLR--QLDFNSDGEKLVLVMKLRGSSKFPPQNMSHNPNGRFVLVCGDGEYDIYTAPA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 421 WRNRSFGSALEFVWSLDG-EYAVRESTSRIKIYsKNFQERKS--IRPPFSAERIFGGVLLAMCTNDFICFHDWAEGRMIR 497
Cdd:cd22938    79 GRNKSFGSAQTFVWVADSrFYALDRMHSSLKIK-KNFKEITSkiVPNCDEIFYAGTGNLLGVDSVDSITFFDWQNKRLLR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 498 RIDVNVKNLYWADSGDLVTIASDTSFYILKYNRDVVSSHLDGGGSVGEEGVEDAFELLHEINERIRTGLWVGDCFIYNNS 577
Cdd:cd22938   158 RIKIKVKYVIWSDDGELVAILAKHSIVILNYLSEKVLAAQETHEGVTEDGIERAFDVLCEIHERVKSGAWVGDVFIYTTS 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 578 SSRLNYCVGGEVTTLFHLDRQMYLLGYLANQSRVYLIDKQFNVVGYTLLLTMIEYKTLVMRGDFDRANALLPSIPKEQHD 657
Cdd:cd22938   238 SNRLNYAVGGGHGIIAHLDLPMYLLGYKGNDNNVYLLDRECRPRVYTIDPTVLEFQTALIRRKYDMADEVLPMVRNAKRT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 658 SVARFLESRGMLEEALEIATDSNYRFDLAVQLGRLEVAKAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAMDLSGL 737
Cdd:cd22938   318 RVAHFLEKQGFKQQALVGSSDIAYLFELALPEGALKIAYQLAHFVKDEKKWFSLALECGSKCNFELALEAAKAANDWEKL 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443060845 738 LLLYSSLGDAEGLTKLTSMAKEQGKNNVAFLCFFMLGKLEECLQLLIESNRIPEAALMSRSYLPSKVPEIVTLWK 812
Cdd:cd22938   398 GLLALLQGNHQIVEMLAQRAENFGKNNKAFFLYLITGKLRKMMKLLIIRKRDMEAAFLNATYLGDQVSERVRIWK 472
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 57-334 1.29e-65

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 222.21  E-value: 1.29e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  57 SVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADDMFIRVYNYNTMDKVKVFEAHT 136
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 137 DYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGwMCTQIFEGHSHYVMQVTFNPkdTNTF-ASASLDRTVKVWSLGSPDPN 215
Cdd:cd00200    94 SYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGTIKLWDLRTGKCV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 216 FTLDGHSKGVNCVDYFTGGDRpyLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLWHS 295
Cdd:cd00200   171 ATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL 248

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1443060845 296 TTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMI 334
Cdd:cd00200   249 RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
46-334 2.04e-59

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 209.00  E-value: 2.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  46 RKLAQRSERAKSVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADDMFIRVYNYNT 125
Cdd:COG2319   114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 126 MDKVKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGWmCTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTVK 205
Cdd:COG2319   194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK-LLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVR 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 206 VWSLGSPDPNFTLDGHSKGVNCVDyFTGgDRPYLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGS 285
Cdd:COG2319   272 LWDLATGELLRTLTGHSGGVNSVA-FSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGS 349

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1443060845 286 EDGTVRLWHSTTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMI 334
Cdd:COG2319   350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 56-293 2.46e-58

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: 201.79  E-value: 2.46e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  56 KSVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADDMFIRVYNYNTMDKVKVFEAH 135
Cdd:cd00200    55 RDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGH 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 136 TDYIRCVAVHPTQPFVLSSSDDMLIKLWDwDKGWMCTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTVKVWSLGSPDPN 215
Cdd:cd00200   135 TDWVNSVAFSPDGTFVASSSQDGTIKLWD-LRTGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTGKCL 212

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443060845 216 FTLDGHSKGVNCVDYFTGGDrpYLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLW 293
Cdd:cd00200   213 GTLRGHENGVNSVAFSPDGY--LLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
40-334 2.90e-56

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 199.75  E-value: 2.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  40 VWWLDQRKLAQR----SERAKSVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADD 115
Cdd:COG2319    62 LLDAAAGALLATllghTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSAD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 116 MFIRVYNYNTMDKVKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGWmCTQIFEGHSHYVMQVTFNPkDTNTF 195
Cdd:COG2319   142 GTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGK-LLRTLTGHTGAVRSVAFSP-DGKLL 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 196 ASASLDRTVKVWSLGSPDPNFTLDGHSKGVNCVDYFTGGDRpyLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFH 275
Cdd:COG2319   220 ASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRL--LASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFS 297

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1443060845 276 PELPIILTGSEDGTVRLWHSTTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMI 334
Cdd:COG2319   298 PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 96-334 5.45e-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: 192.55  E-value: 5.45e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  96 PVRSSKFITRKQWVVAGADDMFIRVYNYNTMDKVKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGwMCTQIF 175
Cdd:cd00200    11 GVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG-ECVRTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 176 EGHSHYVMQVTFNPKDTnTFASASLDRTVKVWSLGSPDPNFTLDGHSKGVNCVDYftGGDRPYLITGSDDQTAKVWDYQT 255
Cdd:cd00200    90 TGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAF--SPDGTFVASSSQDGTIKLWDLRT 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443060845 256 KSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLWHSTTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMI 334
Cdd:cd00200   167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRV 245
WD40 COG2319
WD40 repeat [General function prediction only];
40-297 3.20e-54

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 193.97  E-value: 3.20e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  40 VWWLDQRKLAQR----SERAKSVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADD 115
Cdd:COG2319   146 LWDLATGKLLRTltghSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSAD 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 116 MFIRVYNYNTMDKVKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGwMCTQIFEGHSHYVMQVTFNPkDTNTF 195
Cdd:COG2319   226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG-ELLRTLTGHSGGVNSVAFSP-DGKLL 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 196 ASASLDRTVKVWSLGSPDPNFTLDGHSKGVNCVDYFTGGDRpyLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFH 275
Cdd:COG2319   304 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKT--LASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFS 381

                         250       260
                  ....*....|....*....|..
gi 1443060845 276 PELPIILTGSEDGTVRLWHSTT 297
Cdd:COG2319   382 PDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
45-334 4.71e-53

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 190.89  E-value: 4.71e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  45 QRKLAQRSERAKSVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADDMFIRVYNYN 124
Cdd:COG2319    29 LLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 125 TMDKVKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGWmCTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTV 204
Cdd:COG2319   109 TGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGK-LLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGTV 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 205 KVWSLGSPDPNFTLDGHSKGVNCVDYftGGDRPYLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTG 284
Cdd:COG2319   187 RLWDLATGKLLRTLTGHTGAVRSVAF--SPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASG 264

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1443060845 285 SEDGTVRLWHSTTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMI 334
Cdd:COG2319   265 SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRL 314
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 40-252 1.64e-46

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 168.28  E-value: 1.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  40 VWWLDQRKLAQR----SERAKSVDLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADD 115
Cdd:cd00200    77 LWDLETGECVRTltghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQD 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 116 MFIRVYNYNTMDKVKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGwMCTQIFEGHSHYVMQVTFNPkDTNTF 195
Cdd:cd00200   157 GTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG-KCLGTLRGHENGVNSVAFSP-DGYLL 234

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1443060845 196 ASASLDRTVKVWSLGSPDPNFTLDGHSKGVNCVDYFTGGdrPYLITGSDDQTAKVWD 252
Cdd:cd00200   235 ASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDG--KRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
59-334 1.49e-45

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 169.32  E-value: 1.49e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845  59 DLHPTEPWILSSLYSGSVCIWNYQTQTMVKSFEVTELPVRSSKFITRKQWVVAGADDMFIRVYNYNTMDKVKVFEAHTDY 138
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 139 IRCVAVHPTQPFVLSSSDDMLIKLWDWDKGWmCTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTVKVWSLGSPDPNFTL 218
Cdd:COG2319    81 VLSVAFSPDGRLLASASADGTVRLWDLATGL-LLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLATGKLLRTL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 219 DGHSKGVNCVDYFTGGDRpyLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLWHSTTY 298
Cdd:COG2319   159 TGHSGAVTSVAFSPDGKL--LASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG 236

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1443060845 299 RLENTLNYGLERVWALGYMKGSRRVVIGYDEGTIMI 334
Cdd:COG2319   237 KLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRL 272
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 129-354 2.23e-44

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 162.12  E-value: 2.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 129 VKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWDWDKGWMCTQiFEGHSHYVMQVTFNPkDTNTFASASLDRTVKVWS 208
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA-DGTYLASGSSDKTIRLWD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 209 LGSPDPNFTLDGHSKGVNCVDYFTggDRPYLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDG 288
Cdd:cd00200    80 LETGECVRTLTGHTSYVSSVAFSP--DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443060845 289 TVRLWHSTTYRLENTLnYGLER-VWALGYMKGSRRVVIGYDEGTIMI-KIGREVPVASMDSSGKIIWS 354
Cdd:cd00200   158 TIKLWDLRTGKCVATL-TGHTGeVNSVAFSPDGEKLLSSSSDGTIKLwDLSTGKCLGTLRGHENGVNS 224
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 171-334 1.03e-37

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 143.24  E-value: 1.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 171 CTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTVKVWSLGSPDPNFTLDGHSKGVNCVDYFtgGDRPYLITGSDDQTAKV 250
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAAS--ADGTYLASGSSDKTIRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 251 WDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLWHSTTYRLENTLNYGLERVWALGYMKGSRRVVIGYDEG 330
Cdd:cd00200    78 WDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDG 157


                  ....
gi 1443060845 331 TIMI 334
Cdd:cd00200   158 TIKL 161
WD40 COG2319
WD40 repeat [General function prediction only];
143-453 9.78e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 101.91  E-value: 9.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 143 AVHPTQPFVLSSSDDMLIKLWDWDKGWmCTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTVKVWSLGSPDPNFTLDGHS 222
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGA-LLLLLLGLAAAVASLAASP-DGARLAAGAGDLTLLLLDAAAGALLATLLGHT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 223 KGVNCVDYFTGGDRpyLITGSDDQTAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLWHSTTYRLEN 302
Cdd:COG2319    79 AAVLSVAFSPDGRL--LASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 303 TLNYGLERVWALGYMKGSRRVVIGYDEGTIMI-----------KIGREVPVASMDSS--GKIIWSkhneiqtvniktIGA 369
Cdd:COG2319   157 TLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLwdlatgkllrtLTGHTGAVRSVAFSpdGKLLAS------------GSA 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 370 DNEI-----ADGErlplVVKELGTCDLYPQSLRHNPNGRFVVVCG-DGEYIIY-----TALAWRNRSFGSALEFVWSLDG 438
Cdd:COG2319   225 DGTVrlwdlATGK----LLRTLTGHSGSVRSVAFSPDGRLLASGSaDGTVRLWdlatgELLRTLTGHSGGVNSVAFSPDG 300

                         330
                  ....*....|....*...
gi 1443060845 439 EYAVreSTSR---IKIYS 453
Cdd:COG2319   301 KLLA--SGSDdgtVRLWD 316
Coatomer_WDAD_alpha cd22948
Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called ...
 393-799 8.92e-21

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: 96.43  E-value: 8.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 393 PQSLRHNPNGRFVVVCGDGE------YIIYTALAWRN----RSFGSALEFVWSLDGEYAVRESTSRIKIysKNFQ--ERK 460
Cdd:cd22948    46 PRSLSYNPAENAVLVTSDADggsyelYTLPKDSSGAPekpeSKRGSGLSAVFVARNRFAVLDKSGTILI--KNLEneVTK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 461 SIRPPFSAERIFGG----VLLAmcTNDFICFHDWAEGRMIRRIDV-NVKNLYWADSGDLVTIASDTSFYIlkYNRDvvss 535
Cdd:cd22948   124 KIKPPPNVDKIFYAgtgrVLLR--SEDKVILFDVQQKRVLAEVKVpKVKYVVWSKDMSHVALLSKHSITI--ATKK---- 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 536 hldgggsvgeegvedaFELLHEINE--RIRTGLWVGD-CFIYNNSSsRLNYC-VGGEVTTLFHLDRQMYLLGylANQSRV 611
Cdd:cd22948   196 ----------------LEQLCSVHEtiRIKSGAWDESgVLIYTTLN-HIKYLlPNGDSGIIRTLDSPIYLTR--VKGNTV 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 612 YLIDKQFNVVgyTLLLTMIEY--KTLVMRGDFDRANALLPSiPKEQHDSVARFLESRGMLEEALEIATDSNYRFDLAVQL 689
Cdd:cd22948   257 YCLDREGKVR--VLEIDPTEYlfKLALINKNYDEVLRIIRS-SKLVGQSIIAYLQKKGYPEIALHFVKDPKTRFNLALEC 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 690 GRLEVAKAIAIEAQSESKWRQLGELAMSTGKLDMAEEC-----------LLHAMdlsgllllyssLGDAEGLTKLTSMAK 758
Cdd:cd22948   334 GNLEVALEAAKELDDPECWERLAEEALRQGNHQIVEMAyqktknfdklsFLYLI-----------TGNLEKLRKMLKIAE 402

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1443060845 759 EQGKNNVAFLCFFMLGKLEECLQLLIESNRIPEAALMSRSY 799
Cdd:cd22948   403 KRGDVMSRFQNALYLGDVEERVKILKEAGQLPLAYLTAKTH 443
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 255-294 4.02e-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: 4.02e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1443060845  255 TKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLWH 294
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 258-525 5.76e-10

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 61.58  E-value: 5.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 258 CVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLWHSTTYRLENTLnYGLER-VWALGYMKGSRRVVIGYDEGTIMI-- 334
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL-KGHTGpVRDVAASADGTYLASGSSDKTIRLwd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 335 -KIGREV--------PVASMDssgkiiWSKHNEIqtvnIKTIGADN-----EIADGErlplVVKELGTCDLYPQSLRHNP 400
Cdd:cd00200    80 lETGECVrtltghtsYVSSVA------FSPDGRI----LSSSSRDKtikvwDVETGK----CLTTLRGHTDWVNSVAFSP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 401 NGRFVVVCG-DGeyiiyTALAWRNRSFGSALEFV----------WSLDGE-YAVRESTSRIKIYS-KNFQERKSIR---- 463
Cdd:cd00200   146 DGTFVASSSqDG-----TIKLWDLRTGKCVATLTghtgevnsvaFSPDGEkLLSSSSDGTIKLWDlSTGKCLGTLRghen 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443060845 464 PPFSAERIFGGVLLAMCTNDF-ICFHDWAEGRMIRRI---DVNVKNLYWADSG-DLVTIASDTSFYI 525
Cdd:cd00200   221 GVNSVAFSPDGYLLASGSEDGtIRVWDLRTGECVQTLsghTNSVTSLAWSPDGkRLASGSADGTIRI 287
WD40 pfam00400
WD domain, G-beta repeat;
256-293 4.66e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 52.73  E-value: 4.66e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1443060845 256 KSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRLW 293
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 125-164 5.26e-08

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 49.62  E-value: 5.26e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1443060845  125 TMDKVKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWD 164
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
129-164 9.23e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 48.88  E-value: 9.23e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1443060845 129 VKVFEAHTDYIRCVAVHPTQPFVLSSSDDMLIKLWD 164
Cdd:pfam00400   4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 169-208 6.03e-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: 46.54  E-value: 6.03e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1443060845  169 WMCTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTVKVWS 208
Cdd:smart00320   2 GELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
214-252 2.64e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.03  E-value: 2.64e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1443060845 214 PNFTLDGHSKGVNCVDYFTggDRPYLITGSDDQTAKVWD 252
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSP--DGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
169-208 2.74e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 2.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1443060845 169 WMCTQIFEGHSHYVMQVTFNPkDTNTFASASLDRTVKVWS 208
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 216-252 4.78e-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: 4.78e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1443060845  216 FTLDGHSKGVNCVDYFtgGDRPYLITGSDDQTAKVWD 252
Cdd:smart00320   6 KTLKGHTGPVTSVAFS--PDGKYLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
 174-292 2.13e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.88  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 174 IFEGHSHYVMQVTFNPKDTNTFASASLDRTVKVWSL-------GSPDPNFTLDGHSKGVNCVDyFTGGDRPYLITGSDDQ 246
Cdd:PTZ00421   70 ILLGQEGPIIDVAFNPFDPQKLFTASEDGTIMGWGIpeegltqNISDPIVHLQGHTKKVGIVS-FHPSAMNVLASAGADM 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1443060845 247 TAKVWDYQTKSCVQTLEGHAHNVSAVCFHPELPIILTGSEDGTVRL 292
Cdd:PTZ00421  149 VVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNI 194
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 633-732 3.48e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 41.72  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 633 KTLVMRGDFDRANALLPSIPKEQHDSV------ARFLESRGMLEEALEIA--------TDSNYRFDLAV---QLGRLEVA 695
Cdd:COG4783    12 QALLLAGDYDEAEALLEKALELDPDNPeafallGEILLQLGDLDEAIVLLhealeldpDEPEARLNLGLallKAGDYDEA 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1443060845 696 -----KAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAM 732
Cdd:COG4783    92 lalleKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKAL 133
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 639-733 3.88e-04

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 43.56  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 639 GDFDRANALLPSIPKEQHDSV------ARFLESRGMLEEALEIAT--------DSNYRFDLAV---QLGRLEVA-----K 696
Cdd:COG2956    90 GLLDRAEELLEKLLELDPDDAealrllAEIYEQEGDWEKAIEVLErllklgpeNAHAYCELAElylEQGDYDEAiealeK 169

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1443060845 697 AIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAMD 733
Cdd:COG2956   170 ALKLDPDCARALLLLAELYLEQGDYEEAIAALERALE 206
PTZ00420 PTZ00420
coronin; Provisional
 175-252 4.50e-04

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 43.79  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 175 FEGHSHYVMQVTFNPKDTNTFASASLDRTVKVWSLGS--------PDPNFTLDGHSKGVNCVDYftgGDRPYLITGSD-- 244
Cdd:PTZ00420   70 LKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHndesvkeiKDPQCILKGHKKKISIIDW---NPMNYYIMCSSgf 146


                  ....*...
gi 1443060845 245 DQTAKVWD 252
Cdd:PTZ00420  147 DSFVNIWD 154
PTZ00421 PTZ00421
coronin; Provisional
 114-273 4.91e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 43.73  E-value: 4.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 114 DDMFIRVyNYNTMDKVKVFEaHTDYIRcvaVHPTQPFVL--------------------SSSDDMLIKLWDWDKGWMCTQ 173
Cdd:PTZ00421   39 NDRFIAV-PWQQLGSTAVLK-HTDYGK---LASNPPILLgqegpiidvafnpfdpqklfTASEDGTIMGWGIPEEGLTQN 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 174 I------FEGHSHYVMQVTFNPKDTNTFASASLDRTVKVWSLGSPDPNFTLDGHSKGVNCVDYFTGGDrpYLITGSDDQT 247
Cdd:PTZ00421  114 IsdpivhLQGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGS--LLCTTSKDKK 191

                         170       180
                  ....*....|....*....|....*.
gi 1443060845 248 AKVWDYQTKSCVQTLEGHAHNVSAVC 273
Cdd:PTZ00421  192 LNIIDPRDGTIVSSVEAHASAKSQRC 217
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 669-733 3.19e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.48  E-value: 3.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443060845 669 LEEALEIATDSnyrFDLAVQLGRL-----EVAKAIAI-------EAQSESKWRQLGELAMSTGKLDMAEECLLHAMD 733
Cdd:COG2956    31 LEEALELDPET---VEAHLALGNLyrrrgEYDRAIRIhqkllerDPDRAEALLELAQDYLKAGLLDRAEELLEKLLE 104
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
661-733 3.75e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.46  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 661 RFLESRGMLEEALEIATDS----NYRFDLAVQLGRLEVA----KAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAM 732
Cdd:COG3063     7 DLEEAEEYYEKALELDPDNadalNNLGLLLLEQGRYDEAialeKALKLDPNNAEALLNLAELLLELGDYDEALAYLERAL 86


                  .
gi 1443060845 733 D 733
Cdd:COG3063    87 E 87
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 594-733 4.02e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 39.17  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443060845 594 HLDRQMYLLGYLANQSRVYLIDKQFNVVGYTLLLTMIEYKTLVMRGDFDRANALLPSIPKEQHDSVARFLESRGMLEEAL 673
Cdd:COG5010     2 RALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQAL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443060845 674 EIA-TDSNYRFDLAV---QLGRLEVA-----KAIAIEAQSESKWRQLGELAMSTGKLDMAEECLLHAMD 733
Cdd:COG5010    82 QLDpNNPELYYNLALlysRSGDKDEAkeyyeKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALG 150
 
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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