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Conserved domains on  [gi|18266783|sp|O55029|]
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RecName: Full=Coatomer subunit beta'; AltName: Full=Beta'-coat protein; Short=Beta'-COP; AltName: Full=p102

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', ...
 304-778 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: 931.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 304 PAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMAL 383
Cdd:cd22947   1 PAVSMDSSGKIIWAKHNEIQTANLKALDEEEDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 384 RNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEI 463
Cdd:cd22947  81 RNKAFGSALEFVWSSDSNYYAVRESSSSVKIFKNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRIDV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 464 QPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRL 543
Cdd:cd22947 161 EAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSANRL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 544 NYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAH 623
Cdd:cd22947 241 NYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKVAR 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 624 FLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLA 703
Cdd:cd22947 321 FLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLLLY 400

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18266783 704 TASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLS 778
Cdd:cd22947 401 SSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 8-297 1.39e-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: 227.22  E-value: 1.39e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   8 KRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYN 87
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  88 TLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkdNNQF-ASASLDRT 166
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 167 IKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKpyLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIIT 246
Cdd:cd00200 159 IKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLAS 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 18266783 247 GSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIV 297
Cdd:cd00200 237 GSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 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', ...
 304-778 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: 931.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 304 PAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMAL 383
Cdd:cd22947   1 PAVSMDSSGKIIWAKHNEIQTANLKALDEEEDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 384 RNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEI 463
Cdd:cd22947  81 RNKAFGSALEFVWSSDSNYYAVRESSSSVKIFKNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRIDV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 464 QPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRL 543
Cdd:cd22947 161 EAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSANRL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 544 NYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAH 623
Cdd:cd22947 241 NYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKVAR 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 624 FLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLA 703
Cdd:cd22947 321 FLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLLLY 400

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18266783 704 TASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLS 778
Cdd:cd22947 401 SSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 319-763 0e+00

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 599.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   319 HSEVQQANLKAMGDteiKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAH 398
Cdd:pfam04053   1 ENEVRSYNIKGIEN---KDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   399 dSSEYAIRESNSIVKIFKNFKEK--KSFKPDFGAESIYG---GFLLGVRSVNGLAFYDWENTELIRRIEIQP-KHIFWSD 472
Cdd:pfam04053  78 -RNRFAVLEKSGTVKIFKNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVSPvKYVIWSD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   473 SGELVCIATEESFFILKYLSEKVlaaqethegvtEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSvNRLNYYVGGEIV 552
Cdd:pfam04053 157 DGELVALLSKDTVYILNYNLEAV-----------EDGVEDAFEVLHEISERVKSGAWDGDVFIYTTS-NHLKYLVNGDSG 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   553 TIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSM------ADKVLPtiPKEQRTRVAHFLE 626
Cdd:pfam04053 225 IIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEEvlriirASNLLP--PKDEGQKIIRYLE 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   627 KQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATAS 706
Cdd:pfam04053 303 KKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLST 382

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18266783   707 GNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLP 763
Cdd:pfam04053 383 GNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 8-297 1.39e-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: 227.22  E-value: 1.39e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   8 KRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYN 87
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  88 TLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkdNNQF-ASASLDRT 166
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 167 IKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKpyLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIIT 246
Cdd:cd00200 159 IKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLAS 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 18266783 247 GSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIV 297
Cdd:cd00200 237 GSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
9-297 8.77e-55

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 195.52  E-value: 8.77e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   9 RKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNT 88
Cdd:COG2319 114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  89 LERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIK 168
Cdd:COG2319 194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVR 271

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 169 VWQLGSSSPNFTLEGHEKGVNCIDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGS 248
Cdd:COG2319 272 LWDLATGELLRTLTGHSGGVNSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGS 349

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 18266783 249 EDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIV 297
Cdd:COG2319 350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 218-257 3.33e-10

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 55.78  E-value: 3.33e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 18266783    218 NKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWH 257
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
219-256 1.66e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.89  E-value: 1.66e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 18266783   219 KTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIW 256
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00421 PTZ00421
coronin; Provisional
 145-255 5.94e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 52.97  E-value: 5.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  145 VMQIVINPKDNNQFASASLDRTIKVW-------QLGSSSPNFTLEGHEKGVNCIDYYSGGdKPYLISGADDRLVKIWDYQ 217
Cdd:PTZ00421  78 IIDVAFNPFDPQKLFTASEDGTIMGWgipeeglTQNISDPIVHLQGHTKKVGIVSFHPSA-MNVLASAGADMVVNVWDVE 156

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 18266783  218 NKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRI 255
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', ...
 304-778 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: 931.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 304 PAMSMDANGKIIWAKHSEVQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMAL 383
Cdd:cd22947   1 PAVSMDSSGKIIWAKHNEIQTANLKALDEEEDDDGERLPLSVKDLGSCEIYPQSLQHSPNGRFVAVCGDGEYIIYTALAW 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 384 RNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSFKPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRIEI 463
Cdd:cd22947  81 RNKAFGSALEFVWSSDSNYYAVRESSSSVKIFKNFKERKSFKPPFSAEGIFGGALLGVRSSDFICFYDWETGKLVRRIDV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 464 QPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVNRL 543
Cdd:cd22947 161 EAKNVYWSESGELVAIATDDSFYILRYNRDAVAEALESGEEDEEDGVEDAFEVLHEISESVKSGLWVGDCFIYTNSANRL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 544 NYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRVAH 623
Cdd:cd22947 241 NYYVGGEVVTIAHLDRPMYLLGYLPKDNRVYLIDKDLNVVSYSLSLSVLEYQTAVLRGDFEAADELLPSIPEDQRNKVAR 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 624 FLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLA 703
Cdd:cd22947 321 FLESQGLKELALEVSTDPDHKFELALQLGDLDLALEIARESESESKWKQLGDLALSKGDFDLAEECLKKAGDLSGLLLLY 400

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18266783 704 TASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWRENLS 778
Cdd:cd22947 401 SSTGDKEGLEELAELAEAAGKNNIAFLAYFLLGDLDKCVDLLIKTGRLPEAAFFARTYCPSKVSEVVKLWKEDLR 475
Coatomer_WDAD cd22938
Coatomer WD associated region; The coatomer, which is a cytosolic protein complex that binds ...
 304-776 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: 783.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 304 PAMSMDANGKIIWAKHSEvQQANLKAMGDTEIKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMAL 383
Cdd:cd22938   1 PAYSVDGNGKLHWVKHSE-QQADRFLRQLDFNSDGEKLVLVMKLRGSSKFPPQNMSHNPNGRFVLVCGDGEYDIYTAPAG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 384 RNKSFGSAQEFAWAHDSSEYAIRESNSIVKIFKNFKEKKSF--KPDFGAESIYGGFLLGVRSVNGLAFYDWENTELIRRI 461
Cdd:cd22938  80 RNKSFGSAQTFVWVADSRFYALDRMHSSLKIKKNFKEITSKivPNCDEIFYAGTGNLLGVDSVDSITFFDWQNKRLLRRI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 462 EIQPKHIFWSDSGELVCIATEESFFILKYLSEKVLAAQETHEGVTEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSVN 541
Cdd:cd22938 160 KIKVKYVIWSDDGELVAILAKHSIVILNYLSEKVLAAQETHEGVTEDGIERAFDVLCEIHERVKSGAWVGDVFIYTTSSN 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 542 RLNYYVGGEIVTIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSMADKVLPTIPKEQRTRV 621
Cdd:cd22938 240 RLNYAVGGGHGIIAHLDLPMYLLGYKGNDNNVYLLDRECRPRVYTIDPTVLEFQTALIRRKYDMADEVLPMVRNAKRTRV 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 622 AHFLEKQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLL 701
Cdd:cd22938 320 AHFLEKQGFKQQALVGSSDIAYLFELALPEGALKIAYQLAHFVKDEKKWFSLALECGSKCNFELALEAAKAANDWEKLGL 399

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18266783 702 LATASGNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLPSQVSRVVKLWREN 776
Cdd:cd22938 400 LALLQGNHQIVEMLAQRAENFGKNNKAFFLYLITGKLRKMMKLLIIRKRDMEAAFLNATYLGDQVSERVRIWKEN 474
Coatomer_WDAD pfam04053
Coatomer WD associated region; This region is composed of WD40 repeats.
 319-763 0e+00

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


Pssm-ID: 427679  Cd Length: 439  Bit Score: 599.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   319 HSEVQQANLKAMGDteiKDGERLPLAVKDMGSCEIYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAH 398
Cdd:pfam04053   1 ENEVRSYNIKGIEN---KDGELLSLSLKELGSVEIYPQTLSHNPNGRFVLVCGDGEYIIYTALAWRNKAYGKGLDFVWVS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   399 dSSEYAIRESNSIVKIFKNFKEK--KSFKPDFGAESIYG---GFLLGVRSVNGLAFYDWENTELIRRIEIQP-KHIFWSD 472
Cdd:pfam04053  78 -RNRFAVLEKSGTVKIFKNFKESvtKSIKLPYSVDKIFGggpGSLLGVKSEGSLSFYDWEQGKLVRRIDVSPvKYVIWSD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   473 SGELVCIATEESFFILKYLSEKVlaaqethegvtEDGIEDAFEVLGEIQEIVKTGLWVGDCFIYTSSvNRLNYYVGGEIV 552
Cdd:pfam04053 157 DGELVALLSKDTVYILNYNLEAV-----------EDGVEDAFEVLHEISERVKSGAWDGDVFIYTTS-NHLKYLVNGDSG 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   553 TIAHLDRTMYLLGYIPKDNRLYLGDKELNIVSYSLLVSVLEYQTAVMRRDFSM------ADKVLPtiPKEQRTRVAHFLE 626
Cdd:pfam04053 225 IIKTLDKTLYLLGYLGKENRVYLLDRDGNVVSYEIDPSELEFKLALLRKDYEEvlriirASNLLP--PKDEGQKIIRYLE 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   627 KQGFKQQALTVSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATAS 706
Cdd:pfam04053 303 KKGYPEIALQFVQDPDTRFDLALELGNLDVALEIAKELDDPAKWKRLGDAALSQGNIKLAEEAYQKAKDFDKLLLLYLST 382

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18266783   707 GNASMVNKLAEGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTYLP 763
Cdd:pfam04053 383 GNMEKLKKLAKIAEKRGDYNSAFQNALYLGDVEKCVDILIKTGRLPEAYLFAKTYGP 439
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 8-297 1.39e-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: 227.22  E-value: 1.39e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   8 KRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYN 87
Cdd:cd00200   2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  88 TLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkdNNQF-ASASLDRT 166
Cdd:cd00200  82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTDWVNSVAFSP--DGTFvASSSQDGT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 167 IKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKpyLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIIT 246
Cdd:cd00200 159 IKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEK--LLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLAS 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 18266783 247 GSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIV 297
Cdd:cd00200 237 GSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
9-297 8.77e-55

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 195.52  E-value: 8.77e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   9 RKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNT 88
Cdd:COG2319 114 RTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  89 LERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIK 168
Cdd:COG2319 194 GKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVR 271

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 169 VWQLGSSSPNFTLEGHEKGVNCIDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGS 248
Cdd:COG2319 272 LWDLATGELLRTLTGHSGGVNSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGS 349

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 18266783 249 EDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIV 297
Cdd:COG2319 350 DDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRL 398
WD40 COG2319
WD40 repeat [General function prediction only];
9-260 6.00e-54

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 193.20  E-value: 6.00e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   9 RKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNT 88
Cdd:COG2319 156 RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLAT 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  89 LERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDkKWSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIK 168
Cdd:COG2319 236 GKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVR 313

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 169 VWQLGSSSPNFTLEGHEKGVNCIDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGS 248
Cdd:COG2319 314 LWDLATGKLLRTLTGHTGAVRSVAFSPDGK--TLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGS 391

                       250
                ....*....|..
gi 18266783 249 EDGTVRIWHSST 260
Cdd:COG2319 392 ADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
9-297 3.53e-51

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 185.11  E-value: 3.53e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   9 RKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNT 88
Cdd:COG2319  72 ATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  89 LERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDkKWSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIK 168
Cdd:COG2319 152 GKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA-TGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVR 229

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 169 VWQLGSSSPNFTLEGHEKGVNCIDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGS 248
Cdd:COG2319 230 LWDLATGKLLRTLTGHSGSVRSVAFSPDGR--LLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGS 307

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 18266783 249 EDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIV 297
Cdd:COG2319 308 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
WD40 COG2319
WD40 repeat [General function prediction only];
11-297 3.94e-50

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 182.42  E-value: 3.94e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  11 LTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLE 90
Cdd:COG2319  32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGL 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  91 RVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKkWSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVW 170
Cdd:COG2319 112 LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT-GKLLRTLTGHSGAVTSVAFSP-DGKLLASGSDDGTVRLW 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 171 QLGSSSPNFTLEGHEKGVNCIDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSED 250
Cdd:COG2319 190 DLATGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSAD 267

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 18266783 251 GTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIV 297
Cdd:COG2319 268 GTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRL 314
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 9-215 2.48e-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: 167.90  E-value: 2.48e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   9 RKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNT 88
Cdd:cd00200  87 RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRT 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  89 LERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIK 168
Cdd:cd00200 167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG-KCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIR 244

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 18266783 169 VWQLGSSSPNFTLEGHEKGVNCIDYYsgGDKPYLISGADDRLVKIWD 215
Cdd:cd00200 245 VWDLRTGECVQTLSGHTNSVTSLAWS--PDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
41-297 1.08e-37

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 146.21  E-value: 1.08e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  41 VWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDD 120
Cdd:COG2319  20 LLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASAD 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 121 MLIKLWDWDKKwSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYysGGDKP 200
Cdd:COG2319 100 GTVRLWDLATG-LLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAF--SPDGK 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 201 YLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASL 280
Cdd:COG2319 176 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFS 255

                       250
                ....*....|....*..
gi 18266783 281 RGSNNVALGYDEGSIIV 297
Cdd:COG2319 256 PDGRLLASGSADGTVRL 272
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 8-127 4.25e-20

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: 91.63  E-value: 4.25e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   8 KRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYN 87
Cdd:cd00200 170 VATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLR 249

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18266783  88 TLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWD 127
Cdd:cd00200 250 TGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
Coatomer_WDAD_alpha cd22948
Coatomer WD Associated Region from Coatomer Subunit Alpha; Coatomer subunit alpha, also called ...
 353-761 4.49e-18

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: 87.96  E-value: 4.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 353 IYPQTIQHNPNGRFVVVCGDGEYIIYTAMALRNKSFGSAQEFAWAHDSSEYAI-----------RESNSIVKIFKNfKEK 421
Cdd:cd22948  44 QPPRSLSYNPAENAVLVTSDADGGSYELYTLPKDSSGAPEKPESKRGSGLSAVfvarnrfavldKSGTILIKNLEN-EVT 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 422 KSFKPDFGAESIYG---GFLLgVRSVNGLAFYDWENteliRRI--EIQ---PKHIFWSDSGELVCIATEESFFILkylse 493
Cdd:cd22948 123 KKIKPPPNVDKIFYagtGRVL-LRSEDKVILFDVQQ----KRVlaEVKvpkVKYVVWSKDMSHVALLSKHSITIA----- 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 494 kvlaaqethegvTEDgiedaFEVLGEIQEI--VKTGLWVGD-CFIYTSSvNRLNY-YVGGEIVTIAHLDRTMYLLGYipK 569
Cdd:cd22948 193 ------------TKK-----LEQLCSVHETirIKSGAWDESgVLIYTTL-NHIKYlLPNGDSGIIRTLDSPIYLTRV--K 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 570 DNRLYLGDKE-----LNIVSysllvsvLEYQT--AVMRRDFsmaDKVLPTIpkeqRTR------VAHFLEKQGFKQQALT 636
Cdd:cd22948 253 GNTVYCLDREgkvrvLEIDP-------TEYLFklALINKNY---DEVLRII----RSSklvgqsIIAYLQKKGYPEIALH 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783 637 VSTDPEHRFELALQLGELKIAYQLAVEAESEQKWKQLAELAISKCQFSLAQECLHHAQDYGGLLLLATASGNASMVNKLA 716
Cdd:cd22948 319 FVKDPKTRFNLALECGNLEVALEAAKELDDPECWERLAEEALRQGNHQIVEMAYQKTKNFDKLSFLYLITGNLEKLRKML 398

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 18266783 717 EGAERDGKNNVAFMSYFLQGKLDACLELLIRTGRLPEAAFLARTY 761
Cdd:cd22948 399 KIAEKRGDVMSRFQNALYLGDVEERVKILKEAGQLPLAYLTAKTH 443
WD40 COG2319
WD40 repeat [General function prediction only];
7-129 1.15e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.04  E-value: 1.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   7 IKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNY 86
Cdd:COG2319 280 LLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 18266783  87 NTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWD 129
Cdd:COG2319 360 ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 221-297 3.28e-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: 61.97  E-value: 3.28e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18266783 221 CVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLnYGMER-VWCVASLRGSNNVALGYDEGSIIV 297
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL-KGHTGpVRDVAASADGTYLASGSSDKTIRL 77
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 218-257 3.33e-10

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 55.78  E-value: 3.33e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 18266783    218 NKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWH 257
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
219-256 1.66e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.89  E-value: 1.66e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 18266783   219 KTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIW 256
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 88-127 2.11e-08

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 50.77  E-value: 2.11e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 18266783     88 TLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWD 127
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
90-127 4.33e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 49.65  E-value: 4.33e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 18266783    90 ERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWD 127
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 131-170 1.84e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 48.08  E-value: 1.84e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 18266783    131 KWSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVW 170
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLW 39
PTZ00421 PTZ00421
coronin; Provisional
 145-255 5.94e-07

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 52.97  E-value: 5.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  145 VMQIVINPKDNNQFASASLDRTIKVW-------QLGSSSPNFTLEGHEKGVNCIDYYSGGdKPYLISGADDRLVKIWDYQ 217
Cdd:PTZ00421  78 IIDVAFNPFDPQKLFTASEDGTIMGWgipeeglTQNISDPIVHLQGHTKKVGIVSFHPSA-MNVLASAGADMVVNVWDVE 156

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 18266783  218 NKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRI 255
Cdd:PTZ00421 157 RGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNI 194
WD40 pfam00400
WD domain, G-beta repeat;
175-215 1.19e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 1.19e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 18266783   175 SSPNFTLEGHEKGVNCIDYYSggDKPYLISGADDRLVKIWD 215
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSP--DGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
132-170 2.23e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.03  E-value: 2.23e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 18266783   132 WSCSQVFEGHTHYVMQIVINPkDNNQFASASLDRTIKVW 170
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVW 38
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 156-240 2.69e-06

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 51.24  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  156 NQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDyYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAqNVSCA 235
Cdd:PLN00181 546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSID-YSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKA-NICCV 623


                 ....*
gi 18266783  236 SFHPE 240
Cdd:PLN00181 624 QFPSE 628
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 174-215 2.92e-06

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 44.61  E-value: 2.92e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 18266783    174 SSSPNFTLEGHEKGVNCIDYYSggDKPYLISGADDRLVKIWD 215
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSP--DGKYLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
 138-219 4.53e-05

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 47.25  E-value: 4.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  138 FEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSS--------SPNFTLEGHEKGVNCID-----YYsggdkpYLIS 204
Cdd:PTZ00420  70 LKGHTSSILDLQFNPCFSEILASGSEDLTIRVWEIPHNdesvkeikDPQCILKGHKKKISIIDwnpmnYY------IMCS 143

                         90
                 ....*....|....*
gi 18266783  205 GADDRLVKIWDYQNK 219
Cdd:PTZ00420 144 SGFDSFVNIWDIENE 158
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 69-259 1.50e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 45.46  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783   69 KNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTS-SDDMLIKLWDWDKKWSCSQVfegHTHYVMQ 147
Cdd:PLN00181 545 KSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASgSDDGSVKLWSINQGVSIGTI---KTKANIC 621

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  148 IVINPKDNNQ-FASASLDRTIKVWQLGSSS-PNFTLEGHEKGVNCIDYYsggDKPYLISGADDRLVKIWDYQ------NK 219
Cdd:PLN00181 622 CVQFPSESGRsLAFGSADHKVYYYDLRNPKlPLCTMIGHSKTVSYVRFV---DSSTLVSSSTDNTLKLWDLSmsisgiNE 698

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 18266783  220 TCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSS 259
Cdd:PLN00181 699 TPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKA 738
CDC55 COG5170
Serine/threonine protein phosphatase 2A, regulatory subunit [Signal transduction mechanisms];
97-230 4.78e-04

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


Pssm-ID: 227498 [Multi-domain]  Cd Length: 460  Bit Score: 43.86  E-value: 4.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  97 AHSDYIRCIAVHPTQPFILtSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQI--VIN-----PKDNNQFASASLDRTIKV 169
Cdd:COG5170 170 AHPYHINSISFNSDKETLL-SADDLRINLWNLEIIDGSFNIVDIKPHNMEELteVITsaefhPEMCNVFMYSSSKGEIKL 248

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18266783 170 WQLGSSS----PNFTLEGHEKGVNcIDYYSG----------GDKPYLISGADDRLVKIWDYQN-KTCVQTLEGHAQ 230
Cdd:COG5170 249 NDLRQSAlcdnSKKLFELTIDGVD-VDFFEEivssisdfkfSDNGRYILSRDYLTVKIWDVNMaKNPIKTIPMHCD 323
PTZ00421 PTZ00421
coronin; Provisional
 112-229 1.20e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 42.57  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266783  112 PF----ILTSSDDMLIKLWDWDK---KWSCSQV---FEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTL 181
Cdd:PTZ00421  85 PFdpqkLFTASEDGTIMGWGIPEeglTQNISDPivhLQGHTKKVGIVSFHPSAMNVLASAGADMVVNVWDVERGKAVEVI 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18266783  182 EGHEKGVNCIDYYSGGDkpYLISGADDRLVKIWDYQNKTCVQTLEGHA 229
Cdd:PTZ00421 165 KCHSDQITSLEWNLDGS--LLCTTSKDKKLNIIDPRDGTIVSSVEAHA 210
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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