NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|109019379|ref|XP_001091473|]
View 

DDB1- and CUL4-associated factor 6 isoform X4 [Macaca mulatta]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
43-292 4.38e-22

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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 97.41  E-value: 4.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200   78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200  147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205
                        250
                 ....*....|.
gi 109019379 282 PkdDTARELKT 292
Cdd:cd00200  206 L--STGKCLGT 214
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
750-809 2.23e-05

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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 47.33  E-value: 2.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 750 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 809
Cdd:cd00200  189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
375-670 5.00e-05

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 46.88  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  375 TSQSDISTLPTVPSSPdlegseTAMEVDTPPEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGHH 454
Cdd:pfam17823 122 SPSSAAQSLPAAIAAL------PSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAP 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  455 THHQSDSPSSVVNKQLGSMSldeqqdnnneklspKPGTGEPVLSLHYSTEGTTT----STIKLNFTDEWSSIASSSRGIG 530
Cdd:pfam17823 196 TTAASSAPATLTPARGISTA--------------ATATGHPAAGTALAAVGNSSpaagTVTAAVGTVTPAALATLAAAAG 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  531 SHCKSEGQEESLVPQSSVQPPEGDSETKTPEESSEDVTKYQ-EG----VSAENPVQNHinitqsdkfTAKPSDSNSGERN 605
Cdd:pfam17823 262 TVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQaQGpiiqVSTDQPVHNT---------AGEPTPSPSNTTL 332
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109019379  606 DLNLDSSCGVPEE---STSSEKAKEPETS------DQTSTESATNENNTNPEPQFQTEAIG----PSAHEETSTRDSA 670
Cdd:pfam17823 333 EPNTPKSVASTNLavvTTTKAQAKEPSASpvpvlhTSMIPEVEATSPTTQPSPLLPTQGAAgpgiLLAPEQVATEATA 410
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
43-292 4.38e-22

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: 97.41  E-value: 4.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200   78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200  147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205
                        250
                 ....*....|.
gi 109019379 282 PkdDTARELKT 292
Cdd:cd00200  206 L--STGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
42-292 7.99e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.81  E-value: 7.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319  153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSP--DGKLLASGSADGTVR 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 122 YTNVEqdaetNRQCQFTCHyGTTYEIMTV---PnDPYTFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVA 198
Cdd:COG2319  230 LWDLA-----TGKLLRTLT-GHSGSVRSVafsP-DGRLLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVA 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 199 ICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YI 277
Cdd:COG2319  296 FSPD-GKLLASGSDDGTVRLWDLA---------------TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTV 354
                        250
                 ....*....|....*
gi 109019379 278 YLFDPkdDTARELKT 292
Cdd:COG2319  355 RLWDL--ATGELLRT 367
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
750-809 2.23e-05

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: 47.33  E-value: 2.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 750 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 809
Cdd:cd00200  189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
42-77 4.99e-05

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: 41.14  E-value: 4.99e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 109019379    42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
375-670 5.00e-05

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 46.88  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  375 TSQSDISTLPTVPSSPdlegseTAMEVDTPPEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGHH 454
Cdd:pfam17823 122 SPSSAAQSLPAAIAAL------PSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAP 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  455 THHQSDSPSSVVNKQLGSMSldeqqdnnneklspKPGTGEPVLSLHYSTEGTTT----STIKLNFTDEWSSIASSSRGIG 530
Cdd:pfam17823 196 TTAASSAPATLTPARGISTA--------------ATATGHPAAGTALAAVGNSSpaagTVTAAVGTVTPAALATLAAAAG 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  531 SHCKSEGQEESLVPQSSVQPPEGDSETKTPEESSEDVTKYQ-EG----VSAENPVQNHinitqsdkfTAKPSDSNSGERN 605
Cdd:pfam17823 262 TVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQaQGpiiqVSTDQPVHNT---------AGEPTPSPSNTTL 332
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109019379  606 DLNLDSSCGVPEE---STSSEKAKEPETS------DQTSTESATNENNTNPEPQFQTEAIG----PSAHEETSTRDSA 670
Cdd:pfam17823 333 EPNTPKSVASTNLavvTTTKAQAKEPSASpvpvlhTSMIPEVEATSPTTQPSPLLPTQGAAgpgiLLAPEQVATEATA 410
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
384-669 1.80e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.29  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 384 PTVPSSPDLEGSETAMEVDTPPEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQ-----RQSVEASGHHTHHQ 458
Cdd:NF033609 542 PVVPEQPDEPGEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASdsdsaSDSDSASDSDSASD 621
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 459 SDSPSSVVNKQLGSMSLDEQQDNNNEKLSPKPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGIGSHCKSEGQ 538
Cdd:NF033609 622 SDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 701
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 539 EESLVPQSSVQPPEGDSETKTPEESSEDVTKYQEGVSAENPVQNHINITQSDKFTAKPSDSNSGERNDLNLDSSCGVPEE 618
Cdd:NF033609 702 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 781
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109019379 619 STSSEKAKEPETSDQTSTESATNENNTNPEPQFQTEAIGPSAHEETSTRDS 669
Cdd:NF033609 782 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 832
WD40 pfam00400
WD domain, G-beta repeat;
42-77 3.61e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 3.61e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 109019379   42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
PRK08581 PRK08581
amidase domain-containing protein;
375-654 4.07e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 44.01  E-value: 4.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 375 TSQSDISTLPTVPSSPDLEGSETAMEVDTPPEQFLQPSTSSTMSAQAHSTSSPTESPHSTpllSSPDSEqrqsveasghh 454
Cdd:PRK08581  19 TLTSPTAYADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKF---STIDSS----------- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 455 THHQSDSPSSVVNKQLGSMSLDEQQDNNNEKLSPKPGTGEPVLSLHYSTEGTTTS-TIKLNFTDEWSSIASSSRGIGSHC 533
Cdd:PRK08581  85 TSDSNNIIDFIYKNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPrNSEKSTNDSNKNSDSSIKNDTDTQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 534 KSEGQEESLVPQS---SVQPPEGDSETKTPEESSEDvtkyqegvsaenpvQNHINITQSDKFTAKPSDSNSGERNDLNLD 610
Cdd:PRK08581 165 SSKQDKADNQKAPssnNTKPSTSNKQPNSPKPTQPN--------------QSNSQPASDDTANQKSSSKDNQSMSDSALD 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 109019379 611 SscgVPEEStsSEKAKEPETSDQTSTESATNENNTNPEPQFQTE 654
Cdd:PRK08581 231 S---ILDQY--SEDAKKTQKDYASQSKKDKTETSNTKNPQLPTQ 269
WD40 COG2319
WD40 repeat [General function prediction only];
756-810 8.34e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 8.34e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109019379 756 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 810
Cdd:COG2319  263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
770-809 5.79e-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: 35.37  E-value: 5.79e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 109019379   770 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 809
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
43-292 4.38e-22

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: 97.41  E-value: 4.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200   78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200  147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205
                        250
                 ....*....|.
gi 109019379 282 PkdDTARELKT 292
Cdd:cd00200  206 L--STGKCLGT 214
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
46-275 2.54e-17

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: 83.54  E-value: 2.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  46 TLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDG-VIFYtn 124
Cdd:cd00200   88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLR-GHTDWVNSVAFSP--DGTFVASSSQDGtIKLW-- 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 125 veqDAETNRQCQ-FTCHYGttyEIMTVPNDP--YTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAICP 201
Cdd:cd00200  163 ---DLRTGKCVAtLTGHTG---EVNSVAFSPdgEKLLSSSSDGTIKLWDLS-TGKCLGT------LRGHENGVNSVAFSP 229
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109019379 202 PiPYYLAVGCSDSSVRIYDRRMLGTRATgnyagrgttgmvarfIPSHLNnkscRVTSLCYSEDGQeILVSYSSD 275
Cdd:cd00200  230 D-GYLLASGSEDGTIRVWDLRTGECVQT---------------LSGHTN----SVTSLAWSPDGK-RLASGSAD 282
WD40 COG2319
WD40 repeat [General function prediction only];
42-292 7.99e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.81  E-value: 7.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319  153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSP--DGKLLASGSADGTVR 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 122 YTNVEqdaetNRQCQFTCHyGTTYEIMTV---PnDPYTFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVA 198
Cdd:COG2319  230 LWDLA-----TGKLLRTLT-GHSGSVRSVafsP-DGRLLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVA 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 199 ICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YI 277
Cdd:COG2319  296 FSPD-GKLLASGSDDGTVRLWDLA---------------TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTV 354
                        250
                 ....*....|....*
gi 109019379 278 YLFDPkdDTARELKT 292
Cdd:COG2319  355 RLWDL--ATGELLRT 367
WD40 COG2319
WD40 repeat [General function prediction only];
42-284 5.02e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.11  E-value: 5.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVI- 120
Cdd:COG2319  195 KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT-GHSGSVRSVAFSP--DGRLLASGSADGTVr 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 121 FYtnveqDAETNRQCQ-FTCHYGTTYEIMTVPnDPYTFLSCGEDGTVRWFDTRIKTSCTkedckddILINCRRAATSVAI 199
Cdd:COG2319  272 LW-----DLATGELLRtLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLR-------TLTGHTGAVRSVAF 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 200 cPPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY-IY 278
Cdd:COG2319  339 -SPDGKTLASGSDDGTVRLWDLA---------------TGELLRTLTGHTG----AVTSVAFSPDGR-TLASGSADGtVR 397

                 ....*.
gi 109019379 279 LFDPKD 284
Cdd:COG2319  398 LWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
42-299 1.16e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.96  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319  111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT-GHSGAVTSVAFSP--DGKLLASGSDDGTVR 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 122 YTNVEQDAETNRqcqFTCHygtTYEIMTV---PNDPyTFLSCGEDGTVRWFDTR----IKTsctkedckddiLINCRRAA 194
Cdd:COG2319  188 LWDLATGKLLRT---LTGH---TGAVRSVafsPDGK-LLASGSADGTVRLWDLAtgklLRT-----------LTGHSGSV 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 195 TSVAICPPiPYYLAVGCSDSSVRIYDRrmlgtratgnyagrgTTGMVARFIPSHlnnkSCRVTSLCYSEDGQeILVSYSS 274
Cdd:COG2319  250 RSVAFSPD-GRLLASGSADGTVRLWDL---------------ATGELLRTLTGH----SGGVNSVAFSPDGK-LLASGSD 308
                        250       260
                 ....*....|....*....|....*.
gi 109019379 275 DY-IYLFDPkdDTARELKTPSAEERR 299
Cdd:COG2319  309 DGtVRLWDL--ATGKLLRTLTGHTGA 332
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
42-220 4.20e-15

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 76.60  E-value: 4.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIrSGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:cd00200  126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSP--DGEKLLSSSSDGTIK 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 122 YTNVEQDAETnrqCQFTCHygtTYEIMTV--PNDPYTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAI 199
Cdd:cd00200  203 LWDLSTGKCL---GTLRGH---ENGVNSVafSPDGYLLASGSEDGTIRVWDLR-TGECVQT------LSGHTNSVTSLAW 269
                        170       180
                 ....*....|....*....|.
gi 109019379 200 CPPIPyYLAVGCSDSSVRIYD 220
Cdd:cd00200  270 SPDGK-RLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
43-281 9.00e-15

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 75.83  E-value: 9.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDG-VIF 121
Cdd:cd00200   43 LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT-GHTSYVSSVAFSP--DGRILSSSSRDKtIKV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 122 YtnveqDAETNRQCQ-FTCHYGTtyeIMTVPNDPY-TFLSCG-EDGTVRWFDTRIKTSCTK-EDCKDDIlincrraaTSV 197
Cdd:cd00200  120 W-----DVETGKCLTtLRGHTDW---VNSVAFSPDgTFVASSsQDGTIKLWDLRTGKCVATlTGHTGEV--------NSV 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 198 AICpPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY- 276
Cdd:cd00200  184 AFS-PDGEKLLSSSSDGTIKLWDLS---------------TGKCLGTLRGHEN----GVNSVAFSPDGY-LLASGSEDGt 242

                 ....*
gi 109019379 277 IYLFD 281
Cdd:cd00200  243 IRVWD 247
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
41-170 1.14e-12

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: 69.67  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  41 LKLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVI 120
Cdd:cd00200  167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLR-GHENGVNSVAFSP--DGYLLASGSEDGTI 243
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 109019379 121 -FYtnveqDAETNRQCQ-FTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFD 170
Cdd:cd00200  244 rVW-----DLRTGECVQtLSGHTNSVTSLAWSPDGKR-LASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
750-809 2.23e-05

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: 47.33  E-value: 2.23e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 750 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 809
Cdd:cd00200  189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
42-77 4.99e-05

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: 41.14  E-value: 4.99e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 109019379    42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
375-670 5.00e-05

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 46.88  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  375 TSQSDISTLPTVPSSPdlegseTAMEVDTPPEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGHH 454
Cdd:pfam17823 122 SPSSAAQSLPAAIAAL------PSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAP 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  455 THHQSDSPSSVVNKQLGSMSldeqqdnnneklspKPGTGEPVLSLHYSTEGTTT----STIKLNFTDEWSSIASSSRGIG 530
Cdd:pfam17823 196 TTAASSAPATLTPARGISTA--------------ATATGHPAAGTALAAVGNSSpaagTVTAAVGTVTPAALATLAAAAG 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  531 SHCKSEGQEESLVPQSSVQPPEGDSETKTPEESSEDVTKYQ-EG----VSAENPVQNHinitqsdkfTAKPSDSNSGERN 605
Cdd:pfam17823 262 TVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQaQGpiiqVSTDQPVHNT---------AGEPTPSPSNTTL 332
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109019379  606 DLNLDSSCGVPEE---STSSEKAKEPETS------DQTSTESATNENNTNPEPQFQTEAIG----PSAHEETSTRDSA 670
Cdd:pfam17823 333 EPNTPKSVASTNLavvTTTKAQAKEPSASpvpvlhTSMIPEVEATSPTTQPSPLLPTQGAAgpgiLLAPEQVATEATA 410
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
375-651 5.77e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.83  E-value: 5.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  375 TSQSDISTLPTVPSS-PDLEGSETAMEVDTPPEQFLQPSTSSTmSAQAHSTSSPTESPHSTPLLSSPDSEQRQSVEASGH 453
Cdd:pfam05109 556 TSPTPAVTTPTPNATiPTLGKTSPTSAVTTPTPNATSPTVGET-SPQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQH 634
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  454 HTHHQSDSPSSVVNKQLGSMSLDEQQDNNNEKL----SPKPGTGEPVLSLhySTEGTTTSTIKLNFTDEWSSIASSSRGI 529
Cdd:pfam05109 635 NITSSSTSSMSLRPSSISETLSPSTSDNSTSHMplltSAHPTGGENITQV--TPASTSTHHVSTSSPAPRPGTTSQASGP 712
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379  530 GSHCKSEGQEESLVPQSSvqPPEGDSETKTPEESSEDV-TKYQEGVSAENPVQNHINITQSDKFTAKPSDSNSGERND-- 606
Cdd:pfam05109 713 GNSSTSTKPGEVNVTKGT--PPKNATSPQAPSGQKTAVpTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTpr 790
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 109019379  607 LNLDSSCGVPEESTSSEKAKEPETSDQTSTESATNENNTNPEPQF 651
Cdd:pfam05109 791 TRYNATTYLPPSTSSKLRPRWTFTSPPVTTAQATVPVPPTSQPRF 835
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
384-669 1.80e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.29  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 384 PTVPSSPDLEGSETAMEVDTPPEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLSSPDSEQ-----RQSVEASGHHTHHQ 458
Cdd:NF033609 542 PVVPEQPDEPGEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASdsdsaSDSDSASDSDSASD 621
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 459 SDSPSSVVNKQLGSMSLDEQQDNNNEKLSPKPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGIGSHCKSEGQ 538
Cdd:NF033609 622 SDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 701
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 539 EESLVPQSSVQPPEGDSETKTPEESSEDVTKYQEGVSAENPVQNHINITQSDKFTAKPSDSNSGERNDLNLDSSCGVPEE 618
Cdd:NF033609 702 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 781
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109019379 619 STSSEKAKEPETSDQTSTESATNENNTNPEPQFQTEAIGPSAHEETSTRDS 669
Cdd:NF033609 782 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 832
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
732-809 1.82e-04

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: 44.25  E-value: 1.82e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 109019379 732 VYKGHRNSRTMIKEANfwGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 809
Cdd:cd00200    4 TLKGHTGGVTCVAFSP--DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79
WD40 pfam00400
WD domain, G-beta repeat;
42-77 3.61e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 3.61e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 109019379   42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
PRK08581 PRK08581
amidase domain-containing protein;
375-654 4.07e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 44.01  E-value: 4.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 375 TSQSDISTLPTVPSSPDLEGSETAMEVDTPPEQFLQPSTSSTMSAQAHSTSSPTESPHSTpllSSPDSEqrqsveasghh 454
Cdd:PRK08581  19 TLTSPTAYADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKF---STIDSS----------- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 455 THHQSDSPSSVVNKQLGSMSLDEQQDNNNEKLSPKPGTGEPVLSLHYSTEGTTTS-TIKLNFTDEWSSIASSSRGIGSHC 533
Cdd:PRK08581  85 TSDSNNIIDFIYKNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPrNSEKSTNDSNKNSDSSIKNDTDTQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 534 KSEGQEESLVPQS---SVQPPEGDSETKTPEESSEDvtkyqegvsaenpvQNHINITQSDKFTAKPSDSNSGERNDLNLD 610
Cdd:PRK08581 165 SSKQDKADNQKAPssnNTKPSTSNKQPNSPKPTQPN--------------QSNSQPASDDTANQKSSSKDNQSMSDSALD 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 109019379 611 SscgVPEEStsSEKAKEPETSDQTSTESATNENNTNPEPQFQTE 654
Cdd:PRK08581 231 S---ILDQY--SEDAKKTQKDYASQSKKDKTETSNTKNPQLPTQ 269
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
723-810 4.97e-04

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: 43.09  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 723 NIRRPLVKMVYKGHRNSrtmIKEANF-WGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGI 801
Cdd:cd00200  121 DVETGKCLTTLRGHTDW---VNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS 197

                 ....*....
gi 109019379 802 DYDIKIWSP 810
Cdd:cd00200  198 DGTIKLWDL 206
WD40 COG2319
WD40 repeat [General function prediction only];
756-810 8.34e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 8.34e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109019379 756 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 810
Cdd:COG2319  263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
752-809 1.02e-03

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: 41.94  E-value: 1.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 109019379 752 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 809
Cdd:cd00200   64 TYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
WD40 COG2319
WD40 repeat [General function prediction only];
752-810 1.65e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 41.82  E-value: 1.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 109019379 752 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 810
Cdd:COG2319  343 KTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
756-810 1.83e-03

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: 41.17  E-value: 1.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109019379 756 SGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 810
Cdd:cd00200  111 SSRD-KTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
PRK08581 PRK08581
amidase domain-containing protein;
457-671 3.19e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 41.31  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 457 HQSDSPSSVVNKQLGSmslDEQQDNNNEklspkpgTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSS-------RGI 529
Cdd:PRK08581  26 YADDPQKDSTAKTTSH---DSKKSNDDE-------TSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTsdsnniiDFI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 530 GSHCKSEGQEESLVPQSSvQPPEGDSETKTPEES-SEDVTKYQEGVSAENPVQNhiNITQSDKFTAKPSDSNSGERNDLN 608
Cdd:PRK08581  96 YKNLPQTNINQLLTKNKY-DDNYSLTTLIQNLFNlNSDISDYEQPRNSEKSTND--SNKNSDSSIKNDTDTQSSKQDKAD 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109019379 609 LDSSCGVPEE--STSSEKAKEPETSDQTSTESATNENNTNPEPQFQTEAIGPSAheetSTRDSAL 671
Cdd:PRK08581 173 NQKAPSSNNTkpSTSNKQPNSPKPTQPNQSNSQPASDDTANQKSSSKDNQSMSD----SALDSIL 233
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
289-663 3.52e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 41.25  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 289 ELKTPSAEERREE-LRQPPVKRLRLRGDWSDTGPRARPESErerDGEQSPNVSLMQRM----SDMLSRWFEeasevaQSN 363
Cdd:PRK14949 406 EKKTALTEQTTAQqQVQAANAEAVAEADASAEPADTVEQAL---DDESELLAALNAEQavilSQAQSQGFE------ASS 476
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 364 RGRGRSRPRGGTSQSDISTLPTVPSSPDLEGSETAMEVDTPPEQFLQPSTSSTMSAQAHSTSSPTESPHSTPLLS-SPDS 442
Cdd:PRK14949 477 SLDADNSAVPEQIDSTAEQSVVNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEGDYAQDSAPLDAyQDDY 556
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 443 EQRQSVEASGHHTHHQSDSpssvVNKQLGSMSLDEQQDNNNEKLSPKPGTGE---------PVL----SLhystegttts 509
Cdd:PRK14949 557 VAFSSESYNALSDDEQHSA----NVQSAQSAAEAQPSSQSLSPISAVTTAAAsladddildAVLaardSL---------- 622
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109019379 510 tikLNFTDEWSSIASSSRgigshcKSEGQEESLVPQSSVQPPEGDSETKTPEESSEDVTKYQEGVSAENPVQNHINitQS 589
Cdd:PRK14949 623 ---LSDLDALSPKEGDGK------KSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPE--AA 691
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109019379 590 DKFTAKPSDSNSGERNDL-----NLDSSCGVPEESTSSEKAKEPETSDQTSTESATNENNTNPEPQFQTEAIGPSAHEE 663
Cdd:PRK14949 692 LASGSAPAPPPVPDPYDRppweeAPEVASANDGPNNAAEGNLSESVEDASNSELQAVEQQATHQPQVQAEAQSPASTTA 770
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
752-809 3.77e-03

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: 40.40  E-value: 3.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 109019379 752 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 809
Cdd:cd00200  232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
752-810 4.63e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.28  E-value: 4.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 109019379 752 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 810
Cdd:COG2319  301 KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
770-809 5.79e-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: 35.37  E-value: 5.79e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 109019379   770 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 809
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 COG2319
WD40 repeat [General function prediction only];
756-810 9.08e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 39.51  E-value: 9.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109019379 756 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 810
Cdd:COG2319  221 SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL 275
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH