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Conserved domains on  [gi|242008111|ref|XP_002424856|]
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Coatomer subunit beta', putative [Pediculus humanus corporis]

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', ...
 311-787 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: 899.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 311 PAVSMDvNGGKLIWARHSELQQANLKAMGEDaVVKDGERLPLAVKDMGSCEIYPQTIAHNPNGRFVVVCGDGEYIIYTAM 390
Cdd:cd22947    1 PAVSMD-SSGKIIWAKHNEIQTANLKALDEE-EDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 391 ALRNKAFGSAQEFVWAQDSSEYAIRENSSTVKVFKNFKERKNFKPDFGAEGIFGGYLLGVKSSSGLGLYDWESLELIRRI 470
Cdd:cd22947   79 AWRNKAFGSALEFVWSSDSNYYAVRESSSSVKIFKNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 471 DIQPKHVFWSENGELVCLATEEGYFILKYNQNAVVKARQDKQSITEDGIEDSFEVLGEVHETVKTGLWVGDCFIYTNSVN 550
Cdd:cd22947  159 DVEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSAN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 551 RINYYVGGEIVTIAHLDHTVYLLGYIAKENRLYLGDKELNVVSYSLQLSVLEYQTAVMRQDFAIADRVLPTIPIEYRTRV 630
Cdd:cd22947  239 RLNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKV 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 631 AHFLEKQGFKQQALAVSTDPDHRFDLALQLGQLNTALTLAREAQAQQKWRQLADLAIQRGELTLAQECLHNAQDFGGLLL 710
Cdd:cd22947  319 ARFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLL 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242008111 711 LATASGNAEMIKKLGSSSIENGKNNVGFLSYFLYGDLDKCLDILITTDRLPEAAFFARTYMPSKISYVVELWRESLS 787
Cdd:cd22947  399 LYSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 22-304 2.21e-67

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: 227.60  E-value: 2.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  22 TDRVKCVDLHPTEPWVLSSLYNGIVDVWNHETRQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFNYNTLERVHA 101
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 102 FEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWNWEKQwACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVKVWQLGS 181
Cdd:cd00200   89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKLWDLRT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 182 STPNFTLEGHEKGVNCVDYYHGGDKpyLISGADDRYVKIWDYQNKTCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVR 261
Cdd:cd00200  167 GKCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIR 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 242008111 262 IWHAGTYRLESCLNYGLERVWTIASLRGSNYVSVGYDEGSVLV 304
Cdd:cd00200  245 VWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 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', ...
 311-787 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: 899.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 311 PAVSMDvNGGKLIWARHSELQQANLKAMGEDaVVKDGERLPLAVKDMGSCEIYPQTIAHNPNGRFVVVCGDGEYIIYTAM 390
Cdd:cd22947    1 PAVSMD-SSGKIIWAKHNEIQTANLKALDEE-EDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 391 ALRNKAFGSAQEFVWAQDSSEYAIRENSSTVKVFKNFKERKNFKPDFGAEGIFGGYLLGVKSSSGLGLYDWESLELIRRI 470
Cdd:cd22947   79 AWRNKAFGSALEFVWSSDSNYYAVRESSSSVKIFKNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 471 DIQPKHVFWSENGELVCLATEEGYFILKYNQNAVVKARQDKQSITEDGIEDSFEVLGEVHETVKTGLWVGDCFIYTNSVN 550
Cdd:cd22947  159 DVEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSAN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 551 RINYYVGGEIVTIAHLDHTVYLLGYIAKENRLYLGDKELNVVSYSLQLSVLEYQTAVMRQDFAIADRVLPTIPIEYRTRV 630
Cdd:cd22947  239 RLNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKV 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 631 AHFLEKQGFKQQALAVSTDPDHRFDLALQLGQLNTALTLAREAQAQQKWRQLADLAIQRGELTLAQECLHNAQDFGGLLL 710
Cdd:cd22947  319 ARFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLL 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242008111 711 LATASGNAEMIKKLGSSSIENGKNNVGFLSYFLYGDLDKCLDILITTDRLPEAAFFARTYMPSKISYVVELWRESLS 787
Cdd:cd22947  399 LYSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 327-772 0e+00

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 591.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  327 HSELQQANLKAMGEdavvKDGERLPLAVKDMGSCEIYPQTIAHNPNGRFVVVCGDGEYIIYTAMALRNKAFGSAQEFVWA 406
Cdd:pfam04053   1 ENEVRSYNIKGIEN----KDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  407 qDSSEYAIRENSSTVKVFKNFKER--KNFKPDFGAEGIFG---GYLLGVKSSSGLGLYDWESLELIRRIDIQP-KHVFWS 480
Cdd:pfam04053  77 -SRNRFAVLEKSGTVKIFKNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVSPvKYVIWS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  481 ENGELVCLATEEGYFILKYNQNAVvkarqdkqsitEDGIEDSFEVLGEVHETVKTGLWVGDCFIYTNSvNRINYYVGGEI 560
Cdd:pfam04053 156 DDGELVALLSKDTVYILNYNLEAV-----------EDGVEDAFEVLHEISERVKSGAWDGDVFIYTTS-NHLKYLVNGDS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  561 VTIAHLDHTVYLLGYIAKENRLYLGDKELNVVSYSLQLSVLEYQTAVMRQDFA------IADRVLPtiPIEYRTRVAHFL 634
Cdd:pfam04053 224 GIIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEevlriiRASNLLP--PKDEGQKIIRYL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  635 EKQGFKQQALAVSTDPDHRFDLALQLGQLNTALTLAREAQAQQKWRQLADLAIQRGELTLAQECLHNAQDFGGLLLLATA 714
Cdd:pfam04053 302 EKKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLS 381

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 242008111  715 SGNAEMIKKLGSSSIENGKNNVGFLSYFLYGDLDKCLDILITTDRLPEAAFFARTYMP 772
Cdd:pfam04053 382 TGNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 22-304 2.21e-67

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: 227.60  E-value: 2.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  22 TDRVKCVDLHPTEPWVLSSLYNGIVDVWNHETRQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFNYNTLERVHA 101
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 102 FEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWNWEKQwACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVKVWQLGS 181
Cdd:cd00200   89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKLWDLRT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 182 STPNFTLEGHEKGVNCVDYYHGGDKpyLISGADDRYVKIWDYQNKTCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVR 261
Cdd:cd00200  167 GKCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIR 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 242008111 262 IWHAGTYRLESCLNYGLERVWTIASLRGSNYVSVGYDEGSVLV 304
Cdd:cd00200  245 VWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
16-298 6.06e-58

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 205.15  E-value: 6.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  16 RKLTTRTDRVKCVDLHPTEPWVLSSLYNGIVDVWNHETRQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFNYNT 95
Cdd:COG2319  114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  96 LERVHAFEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWNWEKQwACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVK 175
Cdd:COG2319  194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVR 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 176 VWQLGSSTPNFTLEGHEKGVNCVDYYHGGDkpYLISGADDRYVKIWDYQNKTCVQTLEGHAQNVTAVCFHPELPIVLTGS 255
Cdd:COG2319  272 LWDLATGELLRTLTGHSGGVNSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGS 349

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 242008111 256 EDGTVRIWHAGTYRLESCLNYGLERVWTIA-SLRGSNYVSVGYD 298
Cdd:COG2319  350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAfSPDGRTLASGSAD 393
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 225-264 1.68e-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: 56.94  E-value: 1.68e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 242008111   225 NKTCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVRIWH 264
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
226-263 9.43e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 54.66  E-value: 9.43e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 242008111  226 KTCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVRIW 263
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00421 PTZ00421
coronin; Provisional
 152-262 2.90e-06

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 51.05  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 152 VMQIVINPKDNNTFASASLDRTVKVW-------QLGSSTPNFTLEGHEKGVNCVDYyHGGDKPYLISGADDRYVKIWDYQ 224
Cdd:PTZ00421  78 IIDVAFNPFDPQKLFTASEDGTIMGWgipeeglTQNISDPIVHLQGHTKKVGIVSF-HPSAMNVLASAGADMVVNVWDVE 156

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 242008111 225 NKTCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVRI 262
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', ...
 311-787 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: 899.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 311 PAVSMDvNGGKLIWARHSELQQANLKAMGEDaVVKDGERLPLAVKDMGSCEIYPQTIAHNPNGRFVVVCGDGEYIIYTAM 390
Cdd:cd22947    1 PAVSMD-SSGKIIWAKHNEIQTANLKALDEE-EDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 391 ALRNKAFGSAQEFVWAQDSSEYAIRENSSTVKVFKNFKERKNFKPDFGAEGIFGGYLLGVKSSSGLGLYDWESLELIRRI 470
Cdd:cd22947   79 AWRNKAFGSALEFVWSSDSNYYAVRESSSSVKIFKNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 471 DIQPKHVFWSENGELVCLATEEGYFILKYNQNAVVKARQDKQSITEDGIEDSFEVLGEVHETVKTGLWVGDCFIYTNSVN 550
Cdd:cd22947  159 DVEAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSAN 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 551 RINYYVGGEIVTIAHLDHTVYLLGYIAKENRLYLGDKELNVVSYSLQLSVLEYQTAVMRQDFAIADRVLPTIPIEYRTRV 630
Cdd:cd22947  239 RLNYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKV 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 631 AHFLEKQGFKQQALAVSTDPDHRFDLALQLGQLNTALTLAREAQAQQKWRQLADLAIQRGELTLAQECLHNAQDFGGLLL 710
Cdd:cd22947  319 ARFLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLL 398

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242008111 711 LATASGNAEMIKKLGSSSIENGKNNVGFLSYFLYGDLDKCLDILITTDRLPEAAFFARTYMPSKISYVVELWRESLS 787
Cdd:cd22947  399 LYSSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
Coatomer_WDAD cd22938
Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds ...
 311-784 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: 633.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 311 PAVSMDVNGgKLIWARHSElQQANLKAMGEDAVvKDGERLPLAVKDMGSCEIYPQTIAHNPNGRFVVVCGDGEYIIYTAM 390
Cdd:cd22938    1 PAYSVDGNG-KLHWVKHSE-QQADRFLRQLDFN-SDGEKLVLVMKLRGSSKFPPQNMSHNPNGRFVLVCGDGEYDIYTAP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 391 ALRNKAFGSAQEFVWAQDSSEYAIRENSSTVKVFKNFKERKNF--KPDFGAEGIFGGYLLGVKSSSGLGLYDWESLELIR 468
Cdd:cd22938   78 AGRNKSFGSAQTFVWVADSRFYALDRMHSSLKIKKNFKEITSKivPNCDEIFYAGTGNLLGVDSVDSITFFDWQNKRLLR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 469 RIDIQPKHVFWSENGELVCLATEEGYFILKYNQNAVVKARQDKQSITEDGIEDSFEVLGEVHETVKTGLWVGDCFIYTNS 548
Cdd:cd22938  158 RIKIKVKYVIWSDDGELVAILAKHSIVILNYLSEKVLAAQETHEGVTEDGIERAFDVLCEIHERVKSGAWVGDVFIYTTS 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 549 VNRINYYVGGEIVTIAHLDHTVYLLGYIAKENRLYLGDKELNVVSYSLQLSVLEYQTAVMRQDFAIADRVLPTIPIEYRT 628
Cdd:cd22938  238 SNRLNYAVGGGHGIIAHLDLPMYLLGYKGNDNNVYLLDRECRPRVYTIDPTVLEFQTALIRRKYDMADEVLPMVRNAKRT 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 629 RVAHFLEKQGFKQQALAVSTDPDHRFDLALQLGQLNTALTLAREAQAQQKWRQLADLAIQRGELTLAQECLHNAQDFGGL 708
Cdd:cd22938  318 RVAHFLEKQGFKQQALVGSSDIAYLFELALPEGALKIAYQLAHFVKDEKKWFSLALECGSKCNFELALEAAKAANDWEKL 397

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 242008111 709 LLLATASGNAEMIKKLGSSSIENGKNNVGFLSYFLYGDLDKCLDILITTDRLPEAAFFARTYMPSKISYVVELWRE 784
Cdd:cd22938  398 GLLALLQGNHQIVEMLAQRAENFGKNNKAFFLYLITGKLRKMMKLLIIRKRDMEAAFLNATYLGDQVSERVRIWKE 473
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 327-772 0e+00

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 591.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  327 HSELQQANLKAMGEdavvKDGERLPLAVKDMGSCEIYPQTIAHNPNGRFVVVCGDGEYIIYTAMALRNKAFGSAQEFVWA 406
Cdd:pfam04053   1 ENEVRSYNIKGIEN----KDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  407 qDSSEYAIRENSSTVKVFKNFKER--KNFKPDFGAEGIFG---GYLLGVKSSSGLGLYDWESLELIRRIDIQP-KHVFWS 480
Cdd:pfam04053  77 -SRNRFAVLEKSGTVKIFKNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVSPvKYVIWS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  481 ENGELVCLATEEGYFILKYNQNAVvkarqdkqsitEDGIEDSFEVLGEVHETVKTGLWVGDCFIYTNSvNRINYYVGGEI 560
Cdd:pfam04053 156 DDGELVALLSKDTVYILNYNLEAV-----------EDGVEDAFEVLHEISERVKSGAWDGDVFIYTTS-NHLKYLVNGDS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  561 VTIAHLDHTVYLLGYIAKENRLYLGDKELNVVSYSLQLSVLEYQTAVMRQDFA------IADRVLPtiPIEYRTRVAHFL 634
Cdd:pfam04053 224 GIIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEevlriiRASNLLP--PKDEGQKIIRYL 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  635 EKQGFKQQALAVSTDPDHRFDLALQLGQLNTALTLAREAQAQQKWRQLADLAIQRGELTLAQECLHNAQDFGGLLLLATA 714
Cdd:pfam04053 302 EKKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLS 381

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 242008111  715 SGNAEMIKKLGSSSIENGKNNVGFLSYFLYGDLDKCLDILITTDRLPEAAFFARTYMP 772
Cdd:pfam04053 382 TGNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 22-304 2.21e-67

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: 227.60  E-value: 2.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  22 TDRVKCVDLHPTEPWVLSSLYNGIVDVWNHETRQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFNYNTLERVHA 101
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 102 FEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWNWEKQwACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVKVWQLGS 181
Cdd:cd00200   89 LTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKLWDLRT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 182 STPNFTLEGHEKGVNCVDYYHGGDKpyLISGADDRYVKIWDYQNKTCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVR 261
Cdd:cd00200  167 GKCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIR 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 242008111 262 IWHAGTYRLESCLNYGLERVWTIASLRGSNYVSVGYDEGSVLV 304
Cdd:cd00200  245 VWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
16-298 6.06e-58

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 205.15  E-value: 6.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  16 RKLTTRTDRVKCVDLHPTEPWVLSSLYNGIVDVWNHETRQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFNYNT 95
Cdd:COG2319  114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  96 LERVHAFEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWNWEKQwACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVK 175
Cdd:COG2319  194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVR 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 176 VWQLGSSTPNFTLEGHEKGVNCVDYYHGGDkpYLISGADDRYVKIWDYQNKTCVQTLEGHAQNVTAVCFHPELPIVLTGS 255
Cdd:COG2319  272 LWDLATGELLRTLTGHSGGVNSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGS 349

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 242008111 256 EDGTVRIWHAGTYRLESCLNYGLERVWTIA-SLRGSNYVSVGYD 298
Cdd:COG2319  350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAfSPDGRTLASGSAD 393
WD40 COG2319
WD40 repeat [General function prediction only];
16-267 1.26e-57

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 203.99  E-value: 1.26e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  16 RKLTTRTDRVKCVDLHPTEPWVLSSLYNGIVDVWNHETRQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFNYNT 95
Cdd:COG2319  156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  96 LERVHAFEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWNWEkQWACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVK 175
Cdd:COG2319  236 GKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVR 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 176 VWQLGSSTPNFTLEGHEKGVNCVDYYHGGDkpYLISGADDRYVKIWDYQNKTCVQTLEGHAQNVTAVCFHPELPIVLTGS 255
Cdd:COG2319  314 LWDLATGKLLRTLTGHTGAVRSVAFSPDGK--TLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGS 391

                        250
                 ....*....|..
gi 242008111 256 EDGTVRIWHAGT 267
Cdd:COG2319  392 ADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
16-304 4.75e-55

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 196.67  E-value: 4.75e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  16 RKLTTRTDRVKCVDLHPTEPWVLSSLYNGIVDVWNHETRQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFNYNT 95
Cdd:COG2319   72 ATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  96 LERVHAFEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWNWEKqWACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVK 175
Cdd:COG2319  152 GKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT-GKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVR 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 176 VWQLGSSTPNFTLEGHEKGVNCVDYYHGGDkpYLISGADDRYVKIWDYQNKTCVQTLEGHAQNVTAVCFHPELPIVLTGS 255
Cdd:COG2319  230 LWDLATGKLLRTLTGHSGSVRSVAFSPDGR--LLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGS 307

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 242008111 256 EDGTVRIWHAGTYRLESCLNYGLERVWTIASLRGSNYVSVGYDEGSVLV 304
Cdd:COG2319  308 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
WD40 COG2319
WD40 repeat [General function prediction only];
18-324 2.50e-52

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 188.97  E-value: 2.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  18 LTTRTDRVKCVDLHPTEPWVLSSLYNGIVDVWNHETRQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFNYNTLE 97
Cdd:COG2319   32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  98 RVHAFEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWNWEkQWACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVKVW 177
Cdd:COG2319  112 LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA-TGKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGTVRLW 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 178 QLGSSTPNFTLEGHEKGVNCVDYYHGGDkpYLISGADDRYVKIWDYQNKTCVQTLEGHAQNVTAVCFHPELPIVLTGSED 257
Cdd:COG2319  190 DLATGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSAD 267

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242008111 258 GTVRIWHAGTYRLESCLNYGLERVWTIA-SLRGSNYVSVGYDeGSVLVkvgreepavsMDVNGGKLIW 324
Cdd:COG2319  268 GTVRLWDLATGELLRTLTGHSGGVNSVAfSPDGKLLASGSDD-GTVRL----------WDLATGKLLR 324
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 6-222 4.62e-47

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: 170.21  E-value: 4.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111   6 KIFPLRLD-IKRKLTTRTDRVKCVDLHPTEPWVLSSLYNGIVDVWNHETRQLTKTFEVCDLPVRSARFVPRKNWVITGSD 84
Cdd:cd00200   76 RLWDLETGeCVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQ 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  85 DMQVRVFNYNTLERVHAFEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWNwEKQWACQQVFEGHTHYVMQIVINPkDNNT 164
Cdd:cd00200  156 DGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWD-LSTGKCLGTLRGHENGVNSVAFSP-DGYL 233

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 242008111 165 FASASLDRTVKVWQLGSSTPNFTLEGHEKGVNCVDYYhgGDKPYLISGADDRYVKIWD 222
Cdd:cd00200  234 LASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWS--PDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 99-304 1.85e-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: 162.50  E-value: 1.85e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  99 VHAFEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWNWEKQ------------------------------------W--- 139
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGellrtlkghtgpvrdvaasadgtylasgssdktirlWdle 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 140 --ACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVKVWQLGSSTPNFTLEGHEKGVNCVDYyhGGDKPYLISGADDRY 217
Cdd:cd00200   82 tgECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAF--SPDGTFVASSSQDGT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 218 VKIWDYQNKTCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVRIWHAGTYRLESCLNYGLERVWTIASLRGSNYVSVGY 297
Cdd:cd00200  159 IKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGS 238


                 ....*..
gi 242008111 298 DEGSVLV 304
Cdd:cd00200  239 EDGTIRV 245
WD40 COG2319
WD40 repeat [General function prediction only];
29-324 7.47e-40

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 152.76  E-value: 7.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  29 DLHPTEPWVLSSLYNGIVDVWNHETRQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFNYNTLERVHAFEAHSDY 108
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 109 VRCIAVHPTQPYILTSSDDMLIKLWNWEkQWACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVKVWQLGSSTPNFTL 188
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLA-TGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLATGKLLRTL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 189 EGHEKGVNCVDYyhGGDKPYLISGADDRYVKIWDYQNKTCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVRIWHAGTY 268
Cdd:COG2319  159 TGHSGAVTSVAF--SPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 242008111 269 RLESCLNYGLERVWTIASLRGSNYVSVGYDEGSVLVKvgreepavsmDVNGGKLIW 324
Cdd:COG2319  237 KLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLW----------DLATGELLR 282
Coatomer_WDAD_alpha cd22948
Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called ...
 311-770 7.20e-29

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: 121.09  E-value: 7.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 311 PAvsMDVNGGKLIWARHSELQQANLKAmgedavVKDGERLPLAVKDMGSCEIYPQTIAHNPNGRFVVVCGDGEYIIYTAM 390
Cdd:cd22948    1 PA--FAVHGNSLYYVKDRKLRVYDFSS------GSRVSVPVLSLRGRGGSNQPPRSLSYNPAENAVLVTSDADGGSYELY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 391 ALRNKAFGSAQEFVWAQDSSEYAI-----------RENSSTVKVFKNfKERKNFKPDFGAEGIFG---GYLLgVKSSSGL 456
Cdd:cd22948   73 TLPKDSSGAPEKPESKRGSGLSAVfvarnrfavldKSGTILIKNLEN-EVTKKIKPPPNVDKIFYagtGRVL-LRSEDKV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 457 GLYDWESLELIRRIDIQP-KHVFWSENGELVCLATeegyfilkynqnavvkarqdKQSITedgIED-SFEVLGEVHET-- 532
Cdd:cd22948  151 ILFDVQQKRVLAEVKVPKvKYVVWSKDMSHVALLS--------------------KHSIT---IATkKLEQLCSVHETir 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 533 VKTGLWVGD-CFIYTNSvNRINY-YVGGEIVTIAHLDHTVYLLGyiAKENRLYLGDKELNVVSysLQLSVLEYQT--AVM 608
Cdd:cd22948  208 IKSGAWDESgVLIYTTL-NHIKYlLPNGDSGIIRTLDSPIYLTR--VKGNTVYCLDREGKVRV--LEIDPTEYLFklALI 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 609 RQDFaiaDRVLPTIpieyRTR------VAHFLEKQGFKQQALAVSTDPDHRFDLALQLGQLNTALTLAREAQAQQKWRQL 682
Cdd:cd22948  283 NKNY---DEVLRII----RSSklvgqsIIAYLQKKGYPEIALHFVKDPKTRFNLALECGNLEVALEAAKELDDPECWERL 355

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 683 ADLAIQRGELTLAQECLHNAQDFGGLLLLATASGNAEMIKKLGSSSiENGKNNVGFLSYFLY-GDLDKCLDILITTDRLP 761
Cdd:cd22948  356 AEEALRQGNHQIVEMAYQKTKNFDKLSFLYLITGNLEKLRKMLKIA-EKRGDVMSRFQNALYlGDVEERVKILKEAGQLP 434


                 ....*....
gi 242008111 762 EAAFFARTY 770
Cdd:cd22948  435 LAYLTAKTH 443
WD40 COG2319
WD40 repeat [General function prediction only];
14-136 3.48e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.13  E-value: 3.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  14 IKRKLTTRTDRVKCVDLHPTEPWVLSSLYNGIVDVWNHETRQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFNY 93
Cdd:COG2319  280 LLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 242008111  94 NTLERVHAFEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWNWE 136
Cdd:COG2319  360 ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 225-264 1.68e-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: 56.94  E-value: 1.68e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 242008111   225 NKTCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVRIWH 264
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 228-298 6.56e-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: 61.20  E-value: 6.56e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242008111 228 CVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVRIWHAGTYRLESCLnYGLER-VWTIASLRGSNY-VSVGYD 298
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL-KGHTGpVRDVAASADGTYlASGSSD 72
WD40 pfam00400
WD domain, G-beta repeat;
226-263 9.43e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 54.66  E-value: 9.43e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 242008111  226 KTCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVRIW 263
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 95-134 5.84e-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: 5.84e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 242008111    95 TLERVHAFEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWN 134
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
97-134 1.45e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 48.50  E-value: 1.45e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 242008111   97 ERVHAFEAHSDYVRCIAVHPTQPYILTSSDDMLIKLWN 134
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 138-177 9.54e-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: 46.15  E-value: 9.54e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 242008111   138 QWACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVKVW 177
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
182-222 1.11e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 1.11e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 242008111  182 STPNFTLEGHEKGVNCVDYYHggDKPYLISGADDRYVKIWD 222
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSP--DGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 181-222 2.26e-06

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.00  E-value: 2.26e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 242008111   181 SSTPNFTLEGHEKGVNCVDYYHggDKPYLISGADDRYVKIWD 222
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP--DGKYLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
 152-262 2.90e-06

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 51.05  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 152 VMQIVINPKDNNTFASASLDRTVKVW-------QLGSSTPNFTLEGHEKGVNCVDYyHGGDKPYLISGADDRYVKIWDYQ 224
Cdd:PTZ00421  78 IIDVAFNPFDPQKLFTASEDGTIMGWgipeeglTQNISDPIVHLQGHTKKVGIVSF-HPSAMNVLASAGADMVVNVWDVE 156

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 242008111 225 NKTCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVRI 262
Cdd:PTZ00421 157 RGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNI 194
WD40 pfam00400
WD domain, G-beta repeat;
139-177 3.30e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 3.30e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 242008111  139 WACQQVFEGHTHYVMQIVINPkDNNTFASASLDRTVKVW 177
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVW 38
PTZ00420 PTZ00420
coronin; Provisional
 145-226 5.05e-05

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 47.25  E-value: 5.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 145 FEGHTHYVMQIVINPKDNNTFASASLDRTVKVWQLGSS--------TPNFTLEGHEKGVNCVD-----YYhggdkpYLIS 211
Cdd:PTZ00420  70 LKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNdesvkeikDPQCILKGHKKKISIIDwnpmnYY------IMCS 143

                         90
                 ....*....|....*
gi 242008111 212 GADDRYVKIWDYQNK 226
Cdd:PTZ00420 144 SGFDSFVNIWDIENE 158
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 76-264 5.81e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 47.00  E-value: 5.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111  76 KNWVITGSDDMQVRVFNYNTLERVHAFEAHSDYVRCIAVHPTQPYILTS-SDDMLIKLWNWEKQWACQQVfegHTHYVMQ 154
Cdd:PLN00181 545 KSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASgSDDGSVKLWSINQGVSIGTI---KTKANIC 621

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 155 IVINPKDNN-TFASASLDRTVKVWQL-GSSTPNFTLEGHEKGVNCVDYYhggDKPYLISGADDRYVKIWDYQ------NK 226
Cdd:PLN00181 622 CVQFPSESGrSLAFGSADHKVYYYDLrNPKLPLCTMIGHSKTVSYVRFV---DSSTLVSSSTDNTLKLWDLSmsisgiNE 698

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 242008111 227 TCVQTLEGHAQNVTAVCFHPELPIVLTGSEDGTVRIWH 264
Cdd:PLN00181 699 TPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYH 736
PTZ00421 PTZ00421
coronin; Provisional
 121-243 2.09e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.88  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 121 ILTSSDDMLIKLWNWEKQWACQQV------FEGHTHYVMQIVINPKDNNTFASASLDRTVKVWQLGSSTPNFTLEGHEKG 194
Cdd:PTZ00421  91 LFTASEDGTIMGWGIPEEGLTQNIsdpivhLQGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGKAVEVIKCHSDQ 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 242008111 195 VNCVDYYHGGDkpYLISGADDRYVKIWDYQNKTCVQTLEGHAQNVTAVC 243
Cdd:PTZ00421 171 ITSLEWNLDGS--LLCTTSKDKKLNIIDPRDGTIVSSVEAHASAKSQRC 217
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 166-277 7.53e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 43.54  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 166 ASASLDRTVKVWQLGSSTPNFTLEGHEKGVNCVDyYHGGDKPYLISGADDRYVKIWDYQNKTCVQTLEGHAqNVTAVCFH 245
Cdd:PLN00181 549 ASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSID-YSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKA-NICCVQFP 626

                         90       100       110
                 ....*....|....*....|....*....|...
gi 242008111 246 PELPIVLT-GSEDGTVRIWHAGTYRLESCLNYG 277
Cdd:PLN00181 627 SESGRSLAfGSADHKVYYYDLRNPKLPLCTMIG 659
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 53-92 1.72e-03

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: 36.91  E-value: 1.72e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 242008111    53 TRQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFN 92
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
104-243 3.41e-03

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


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 41.17  E-value: 3.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 104 AHSDYVRCIAVHPTQPYILtSSDDMLIKLWNWEKQWACQQVFEGHTHYVMQI--VIN-----PKDNNTFASASLDRTVKV 176
Cdd:COG5170  170 AHPYHINSISFNSDKETLL-SADDLRINLWNLEIIDGSFNIVDIKPHNMEELteVITsaefhPEMCNVFMYSSSKGEIKL 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242008111 177 WQLGSST----PNFTLEGHEKGVNcVDYYHG----------GDKPYLISGADDRYVKIWDYQN-KTCVQTLEGHAQNVTA 241
Cdd:COG5170  249 NDLRQSAlcdnSKKLFELTIDGVD-VDFFEEivssisdfkfSDNGRYILSRDYLTVKIWDVNMaKNPIKTIPMHCDLMDE 327


                 ..
gi 242008111 242 VC 243
Cdd:COG5170  328 LN 329
WD40 pfam00400
WD domain, G-beta repeat;
54-92 4.03e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 4.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 242008111   54 RQLTKTFEVCDLPVRSARFVPRKNWVITGSDDMQVRVFN 92
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
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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