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Conserved domains on  [gi|966923742|ref|XP_014980672|]
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DDB1- and CUL4-associated factor 6 isoform X2 [Macaca mulatta]

Protein Classification

Graphical summary

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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 2.36e-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: 98.18  E-value: 2.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200   78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200  147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                        250
                 ....*....|.
gi 966923742 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 ...
 807-866 1.94e-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: 1.94e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 807 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200  189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
PRK08581 super family cl35718
amidase domain-containing protein;
509-728 3.61e-04

amidase domain-containing protein;


The actual alignment was detected with superfamily member PRK08581:

Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 44.39  E-value: 3.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 509 SSQDPHASDSPSSVVNKQLGSmslDEQQDNNNEklspkpgTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSS----- 583
Cdd:PRK08581  21 TSPTAYADDPQKDSTAKTTSH---DSKKSNDDE-------TSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTsdsnn 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 584 --RGIGSHCKSEGQEESLVPQSSVQPPEGDSETKTPEESSEDVTKYQEGVSAENPVQNhiNITQSDKFTAKPSDSNSGER 661
Cdd:PRK08581  91 iiDFIYKNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTND--SNKNSDSSIKNDTDTQSSKQ 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966923742 662 NDLNLDSSCGVPEE--STSSEKAKEPETSDQTSTESATNENNTNPEPQFQTEAIGPSAheetSTRDSAL 728
Cdd:PRK08581 169 DKADNQKAPSSNNTkpSTSNKQPNSPKPTQPNQSNSQPASDDTANQKSSSKDNQSMSD----SALDSIL 233
 
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 2.36e-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: 98.18  E-value: 2.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200   78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200  147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                        250
                 ....*....|.
gi 966923742 282 PkdDTARELKT 292
Cdd:cd00200  206 L--STGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
42-292 8.74e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.81  E-value: 8.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319  153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSP--DGKLLASGSADGTVR 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 122 YTNVEqdaetNRQCQFTCHyGTTYEIMTV---PnDPYTFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVA 198
Cdd:COG2319  230 LWDLA-----TGKLLRTLT-GHSGSVRSVafsP-DGRLLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVA 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 199 ICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YI 277
Cdd:COG2319  296 FSPD-GKLLASGSDDGTVRLWDLA---------------TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTV 354

                        250
                 ....*....|....*
gi 966923742 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 ...
 807-866 1.94e-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: 1.94e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 807 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200  189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 42-77 4.28e-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: 41.53  E-value: 4.28e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 966923742    42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
WD40 pfam00400
WD domain, G-beta repeat;
42-77 2.98e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 2.98e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 966923742   42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
PRK08581 PRK08581
amidase domain-containing protein;
509-728 3.61e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 44.39  E-value: 3.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 509 SSQDPHASDSPSSVVNKQLGSmslDEQQDNNNEklspkpgTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSS----- 583
Cdd:PRK08581  21 TSPTAYADDPQKDSTAKTTSH---DSKKSNDDE-------TSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTsdsnn 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 584 --RGIGSHCKSEGQEESLVPQSSVQPPEGDSETKTPEESSEDVTKYQEGVSAENPVQNhiNITQSDKFTAKPSDSNSGER 661
Cdd:PRK08581  91 iiDFIYKNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTND--SNKNSDSSIKNDTDTQSSKQ 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966923742 662 NDLNLDSSCGVPEE--STSSEKAKEPETSDQTSTESATNENNTNPEPQFQTEAIGPSAheetSTRDSAL 728
Cdd:PRK08581 169 DKADNQKAPSSNNTkpSTSNKQPNSPKPTQPNQSNSQPASDDTANQKSSSKDNQSMSD----SALDSIL 233
WD40 COG2319
WD40 repeat [General function prediction only];
813-867 8.99e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 8.99e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 966923742 813 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 867
Cdd:COG2319  263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 546-726 2.14e-03

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: 41.82  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 546 KPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGIGSHCKSEGQEESLVPQSSVQPPEGDSETKTPEESSEDVT 625
Cdd:NF033609 550 EPGEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSD 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 626 KYQEGVSAENPVQNHINITQSDKFTAKPSDSNSGERNDLNLDSSCGVPEESTSSEKAKEPETSDQTSTESATNENNTNPE 705
Cdd:NF033609 630 SASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 709

                        170       180
                 ....*....|....*....|.
gi 966923742 706 PQFQTEAIGPSAHEETSTRDS 726
Cdd:NF033609 710 SDSDSDSDSDSDSDSDSDSDS 730
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 827-866 5.11e-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: 35.75  E-value: 5.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 966923742   827 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
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 2.36e-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: 98.18  E-value: 2.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTiRSGHRANIFSAKFLPctNDKQIVSCSGDGVIFY 122
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT-LKGHTGPVRDVAASA--DGTYLASGSSDKTIRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 123 TNVEQDAETNRqcqFTCHYGTTYEIMTVPNDPYtFLSCGEDGTVRWFDTRIKTSCTKEDCKDDilincrrAATSVAICPP 202
Cdd:cd00200   78 WDLETGECVRT---LTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETGKCLTTLRGHTD-------WVNSVAFSPD 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 203 iPYYLAVGCSDSSVRIYDrrmlgtratgnyagrGTTGMVARFIPSHlnnkSCRVTSLCYSEDGQEILVSySSDY-IYLFD 281
Cdd:cd00200  147 -GTFVASSSQDGTIKLWD---------------LRTGKCVATLTGH----TGEVNSVAFSPDGEKLLSS-SSDGtIKLWD 205

                        250
                 ....*....|.
gi 966923742 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 1.41e-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: 84.31  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742  46 TLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDG-VIFYtn 124
Cdd:cd00200   88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLR-GHTDWVNSVAFSP--DGTFVASSSQDGtIKLW-- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 125 veqDAETNRQCQ-FTCHYGttyEIMTVPNDP--YTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAICP 201
Cdd:cd00200  163 ---DLRTGKCVAtLTGHTG---EVNSVAFSPdgEKLLSSSSDGTIKLWDLS-TGKCLGT------LRGHENGVNSVAFSP 229

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966923742 202 PiPYYLAVGCSDSSVRIYDRRMLGTRATgnyagrgttgmvarfIPSHLNnkscRVTSLCYSEDGQeILVSYSSD 275
Cdd:cd00200  230 D-GYLLASGSEDGTIRVWDLRTGECVQT---------------LSGHTN----SVTSLAWSPDGK-RLASGSAD 282
WD40 COG2319
WD40 repeat [General function prediction only];
42-292 8.74e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 83.81  E-value: 8.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319  153 KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-GHTGAVRSVAFSP--DGKLLASGSADGTVR 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 122 YTNVEqdaetNRQCQFTCHyGTTYEIMTV---PnDPYTFLSCGEDGTVRWFDTRiktscTKEDCKddILINCRRAATSVA 198
Cdd:COG2319  230 LWDLA-----TGKLLRTLT-GHSGSVRSVafsP-DGRLLASGSADGTVRLWDLA-----TGELLR--TLTGHSGGVNSVA 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 199 ICPPiPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSD-YI 277
Cdd:COG2319  296 FSPD-GKLLASGSDDGTVRLWDLA---------------TGKLLRTLTGHTG----AVRSVAFSPDGK-TLASGSDDgTV 354

                        250
                 ....*....|....*
gi 966923742 278 YLFDPkdDTARELKT 292
Cdd:COG2319  355 RLWDL--ATGELLRT 367
WD40 COG2319
WD40 repeat [General function prediction only];
42-284 5.48e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.11  E-value: 5.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVI- 120
Cdd:COG2319  195 KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT-GHSGSVRSVAFSP--DGRLLASGSADGTVr 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 121 FYtnveqDAETNRQCQ-FTCHYGTTYEIMTVPnDPYTFLSCGEDGTVRWFDTRIKTSCTkedckddILINCRRAATSVAI 199
Cdd:COG2319  272 LW-----DLATGELLRtLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLR-------TLTGHTGAVRSVAF 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 200 cPPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY-IY 278
Cdd:COG2319  339 -SPDGKTLASGSDDGTVRLWDLA---------------TGELLRTLTGHTG----AVTSVAFSPDGR-TLASGSADGtVR 397


                 ....*.
gi 966923742 279 LFDPKD 284
Cdd:COG2319  398 LWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
42-299 1.26e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.96  E-value: 1.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:COG2319  111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT-GHSGAVTSVAFSP--DGKLLASGSDDGTVR 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 122 YTNVEQDAETNRqcqFTCHygtTYEIMTV---PNDPyTFLSCGEDGTVRWFDTR----IKTsctkedckddiLINCRRAA 194
Cdd:COG2319  188 LWDLATGKLLRT---LTGH---TGAVRSVafsPDGK-LLASGSADGTVRLWDLAtgklLRT-----------LTGHSGSV 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 195 TSVAICPPiPYYLAVGCSDSSVRIYDRrmlgtratgnyagrgTTGMVARFIPSHlnnkSCRVTSLCYSEDGQeILVSYSS 274
Cdd:COG2319  250 RSVAFSPD-GRLLASGSADGTVRLWDL---------------ATGELLRTLTGH----SGGVNSVAFSPDGK-LLASGSD 308

                        250       260
                 ....*....|....*....|....*.
gi 966923742 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 2.78e-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: 77.38  E-value: 2.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742  42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIrSGHRANIFSAKFLPctNDKQIVSCSGDGVIF 121
Cdd:cd00200  126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATL-TGHTGEVNSVAFSP--DGEKLLSSSSDGTIK 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 122 YTNVEQDAETnrqCQFTCHygtTYEIMTV--PNDPYTFLSCGEDGTVRWFDTRiKTSCTKEdckddiLINCRRAATSVAI 199
Cdd:cd00200  203 LWDLSTGKCL---GTLRGH---ENGVNSVafSPDGYLLASGSEDGTIRVWDLR-TGECVQT------LSGHTNSVTSLAW 269

                        170       180
                 ....*....|....*....|.
gi 966923742 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 ...
 43-292 5.09e-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: 5.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742  43 LEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDG-VIF 121
Cdd:cd00200   43 LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT-GHTSYVSSVAFSP--DGRILSSSSRDKtIKV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 122 YtnveqDAETNRQCQ-FTCHYGTtyeIMTVPNDPY-TFLSCG-EDGTVRWFDTRIKTSCTK-EDCKDDIlincrraaTSV 197
Cdd:cd00200  120 W-----DVETGKCLTtLRGHTDW---VNSVAFSPDgTFVASSsQDGTIKLWDLRTGKCVATlTGHTGEV--------NSV 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 198 AICpPIPYYLAVGCSDSSVRIYDRRmlgtratgnyagrgtTGMVARFIPSHLNnkscRVTSLCYSEDGQeILVSYSSDY- 276
Cdd:cd00200  184 AFS-PDGEKLLSSSSDGTIKLWDLS---------------TGKCLGTLRGHEN----GVNSVAFSPDGY-LLASGSEDGt 242

                        250
                 ....*....|....*.
gi 966923742 277 IYLFDpkDDTARELKT 292
Cdd:cd00200  243 IRVWD--LRTGECVQT 256
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 41-170 8.06e-13

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: 70.06  E-value: 8.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742  41 LKLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVISNPYSRKVLTTIRsGHRANIFSAKFLPctNDKQIVSCSGDGVI 120
Cdd:cd00200  167 GKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLR-GHENGVNSVAFSP--DGYLLASGSEDGTI 243

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 966923742 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 ...
 807-866 1.94e-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: 1.94e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 807 GANFVMSGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200  189 GEKLLSSSSD-GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD 247
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 42-77 4.28e-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: 41.53  E-value: 4.28e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 966923742    42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKL 38
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 789-866 1.62e-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: 44.63  E-value: 1.62e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966923742 789 VYKGHRNSRTMIKEANfwGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200    4 TLKGHTGGVTCVAFSP--DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD 79
WD40 pfam00400
WD domain, G-beta repeat;
42-77 2.98e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 2.98e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 966923742   42 KLEATLNVHDGCVNTICWNDTGEYILSGSDDTKLVI 77
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKV 37
PRK08581 PRK08581
amidase domain-containing protein;
509-728 3.61e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 44.39  E-value: 3.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 509 SSQDPHASDSPSSVVNKQLGSmslDEQQDNNNEklspkpgTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSS----- 583
Cdd:PRK08581  21 TSPTAYADDPQKDSTAKTTSH---DSKKSNDDE-------TSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTsdsnn 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 584 --RGIGSHCKSEGQEESLVPQSSVQPPEGDSETKTPEESSEDVTKYQEGVSAENPVQNhiNITQSDKFTAKPSDSNSGER 661
Cdd:PRK08581  91 iiDFIYKNLPQTNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYEQPRNSEKSTND--SNKNSDSSIKNDTDTQSSKQ 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966923742 662 NDLNLDSSCGVPEE--STSSEKAKEPETSDQTSTESATNENNTNPEPQFQTEAIGPSAheetSTRDSAL 728
Cdd:PRK08581 169 DKADNQKAPSSNNTkpSTSNKQPNSPKPTQPNQSNSQPASDDTANQKSSSKDNQSMSD----SALDSIL 233
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 780-867 4.18e-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: 43.48  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 780 NIRRPLVKMVYKGHRNSrtmIKEANF-WGANFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGI 858
Cdd:cd00200  121 DVETGKCLTTLRGHTDW---VNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS 197


                 ....*....
gi 966923742 859 DYDIKIWSP 867
Cdd:cd00200  198 DGTIKLWDL 206
WD40 COG2319
WD40 repeat [General function prediction only];
813-867 8.99e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.59  E-value: 8.99e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 966923742 813 SGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 867
Cdd:COG2319  263 SGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 809-866 9.77e-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: 42.32  E-value: 9.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 966923742 809 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200   64 TYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 813-867 1.63e-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: 41.55  E-value: 1.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 966923742 813 SGSDcGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 867
Cdd:cd00200  111 SSRD-KTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL 164
WD40 COG2319
WD40 repeat [General function prediction only];
809-867 1.78e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 41.82  E-value: 1.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 966923742 809 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 867
Cdd:COG2319  343 KTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 546-726 2.14e-03

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: 41.82  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 546 KPGTGEPVLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGIGSHCKSEGQEESLVPQSSVQPPEGDSETKTPEESSEDVT 625
Cdd:NF033609 550 EPGEIEPIPEDSDSDPGSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSD 629

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 626 KYQEGVSAENPVQNHINITQSDKFTAKPSDSNSGERNDLNLDSSCGVPEESTSSEKAKEPETSDQTSTESATNENNTNPE 705
Cdd:NF033609 630 SASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 709

                        170       180
                 ....*....|....*....|.
gi 966923742 706 PQFQTEAIGPSAHEETSTRDS 726
Cdd:NF033609 710 SDSDSDSDSDSDSDSDSDSDS 730
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 809-866 3.49e-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: 3.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 966923742 809 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:cd00200  232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
809-867 4.98e-03

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 40.28  E-value: 4.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 966923742 809 NFVMSGSDCGHIFIWDRHTAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWSP 867
Cdd:COG2319  301 KLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDL 359
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 827-866 5.11e-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: 35.75  E-value: 5.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 966923742   827 TAEHLMLLEADNHVVNCLQPHPFDPILASSGIDYDIKIWS 866
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 396-720 8.37e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 40.09  E-value: 8.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 396 ETAMEVDTPPEQFLQPSTSSTM-----------SAQAHSTSSPTESPHSTPLLSSPDSEQR-QSVEASGHHTHHQSEFlr 463
Cdd:PRK14949 369 DDPAEISLPEGQTPSALAAAVQaphanepqfvnAAPAEKKTALTEQTTAQQQVQAANAEAVaEADASAEPADTVEQAL-- 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 464 GPEIALLrKRL---QQLRLKKAEQQ----------RQQELAAHTQQQPSTS------------DQSSHEGSSQDPHASDS 518
Cdd:PRK14949 447 DDESELL-AALnaeQAVILSQAQSQgfeasssldaDNSAVPEQIDSTAEQSvvnpsvtdtqvdDTSASNNSAADNTVDDN 525

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 519 PS---SVVNKQLGSM-------SLDEQQDNNNEKLSPKPGTGEPvLSLHYSTEGTTTSTIKLNFTDEWSSIASSSRGI-- 586
Cdd:PRK14949 526 YSaedTLESNGLDEGdyaqdsaPLDAYQDDYVAFSSESYNALSD-DEQHSANVQSAQSAAEAQPSSQSLSPISAVTTAaa 604

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 587 -----------------------------GSHCKSEGQEESLVPQSSVQPPEGDSETKTPEESSEDVTKYQEGVSAENPV 637
Cdd:PRK14949 605 sladddildavlaardsllsdldalspkeGDGKKSSADRKPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATH 684

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 638 QNHINitQSDKFTAKPSDSNSGERNDL-----NLDSSCGVPEESTSSEKAKEPETSDQTSTESATNENNTNPEPQFQTEA 712
Cdd:PRK14949 685 QSVPE--AALASGSAPAPPPVPDPYDRppweeAPEVASANDGPNNAAEGNLSESVEDASNSELQAVEQQATHQPQVQAEA 762


                 ....*...
gi 966923742 713 IGPSAHEE 720
Cdd:PRK14949 763 QSPASTTA 770
PRK08581 PRK08581
amidase domain-containing protein;
492-711 9.27e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 39.77  E-value: 9.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 492 AHTQQQPSTSDQSSHEGSSQDPHASDSPSSVVNKqlgsmslDEQQDNNNEKLSPKPGTGEPVLSLHYSTEGTTTSTIKLN 571
Cdd:PRK08581  34 STAKTTSHDSKKSNDDETSKDTSSKDTDKADNNN-------TSNQDNNDKKFSTIDSSTSDSNNIIDFIYKNLPQTNINQ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 572 F------------TDEWSSIASSSRGIGSHCKSEGQEESLVPQSS--------VQPPEGDSETKTPEESSEDVTKYQEGV 631
Cdd:PRK08581 107 LltknkyddnyslTTLIQNLFNLNSDISDYEQPRNSEKSTNDSNKnsdssiknDTDTQSSKQDKADNQKAPSSNNTKPST 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966923742 632 SAE--------NPVQNHINITQSDKFTAKPSDSNSGERNDLNLDSscgVPEEStsSEKAKEPETSDQTSTESATNENNTN 703
Cdd:PRK08581 187 SNKqpnspkptQPNQSNSQPASDDTANQKSSSKDNQSMSDSALDS---ILDQY--SEDAKKTQKDYASQSKKDKTETSNT 261


                 ....*...
gi 966923742 704 PEPQFQTE 711
Cdd:PRK08581 262 KNPQLPTQ 269
 
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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