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Conserved domains on  [gi|1955810733|ref|XP_038857587|]
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activating molecule in BECN1-regulated autophagy protein 1-like isoform X2 [Salvelinus namaycush]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
59-198 5.58e-19

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.13  E-value: 5.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   59 LAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTipG-LVASGCLDGEVRIWDLHGGSESW-FTES 136
Cdd:COG2319    168 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPD--GkLLASGSADGTVRLWDLATGKLLRtLTGH 245

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955810733  137 NVAIASLTFHPTAQLLLIAT-NNELHFWDWSRPEPFAVVktGSETERVRLVRFDPLGHNLLTA 198
Cdd:COG2319    246 SGSVRSVAFSPDGRLLASGSaDGTVRLWDLATGELLRTL--TGHSGGVNSVAFSPDGKLLASG 306
PHA03269 super family cl29788
envelope glycoprotein C; Provisional
 641-765 1.13e-03

envelope glycoprotein C; Provisional


The actual alignment was detected with superfamily member PHA03269:

Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.56  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733  641 RTSPASSTSAVSTQEGSSSPWRQPPSPAYEEPHASSRSRDPHPHPQERERRVAQP---PEPS---ELQPSPGPHVAAM-- 712
Cdd:PHA03269    16 NLIIANLNTNIPIPELHTSAATQKPDPAPAPHQAASRAPDPAVAPTSAASRKPDLaqaPTPAaseKFDPAPAPHQAASra 95

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1955810733  713 PFPTIASSSAQPGEQTVGLVFNQETGQWERVYRQATSSRSADAPPEALSQEMP 765
Cdd:PHA03269    96 PDPAVAPQLAAAPKPDAAEAFTSAAQAHEAPADAGTSAASKKPDPAAHTQHSP 148
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 310-422 2.04e-03

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733  310 SPSLGESPSTSRPVVHPELPQVASQPAPHASTFSartEPRQPSEPTGAQQRPSAfttvyySAGSSLHRAVPTTHVASQPL 389
Cdd:PRK10263   746 TPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQ---QPQQPVAPQPQYQQPQQ------PVAPQPQYQQPQQPVAPQPQ 816

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1955810733  390 SQQ----LLPPPTIHQHQPPSRPLPGPDWTRSLLnMR 422
Cdd:PRK10263   817 YQQpqqpVAPQPQYQQPQQPVAPQPQDTLLHPLL-MR 852
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
59-198 5.58e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.13  E-value: 5.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   59 LAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTipG-LVASGCLDGEVRIWDLHGGSESW-FTES 136
Cdd:COG2319    168 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPD--GkLLASGSADGTVRLWDLATGKLLRtLTGH 245

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955810733  137 NVAIASLTFHPTAQLLLIAT-NNELHFWDWSRPEPFAVVktGSETERVRLVRFDPLGHNLLTA 198
Cdd:COG2319    246 SGSVRSVAFSPDGRLLASGSaDGTVRLWDLATGELLRTL--TGHSGGVNSVAFSPDGKLLASG 306
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 59-198 1.43e-18

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: 87.78  E-value: 1.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   59 LAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTIPGLVASGClDGEVRIWDLHGGSES-WFTESN 137
Cdd:cd00200    141 VAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDLSTGKCLgTLRGHE 219

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955810733  138 VAIASLTFHPTAQLLLIAT-NNELHFWDWSRPEPfavVKTGSE-TERVRLVRFDPLGHNLLTA 198
Cdd:cd00200    220 NGVNSVAFSPDGYLLASGSeDGTIRVWDLRTGEC---VQTLSGhTNSVTSLAWSPDGKRLASG 279
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 84-124 9.62e-08

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 49.62  E-value: 9.62e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1955810733    84 TGKCLHSLVGHRRTPWCVTFHPTIPgLVASGCLDGEVRIWD 124
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGK-YLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
85-124 5.80e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 5.80e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1955810733   85 GKCLHSLVGHRRTPWCVTFHPTiPGLVASGCLDGEVRIWD 124
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPD-GKLLASGSDDGTVKVWD 39
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 641-765 1.13e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.56  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733  641 RTSPASSTSAVSTQEGSSSPWRQPPSPAYEEPHASSRSRDPHPHPQERERRVAQP---PEPS---ELQPSPGPHVAAM-- 712
Cdd:PHA03269    16 NLIIANLNTNIPIPELHTSAATQKPDPAPAPHQAASRAPDPAVAPTSAASRKPDLaqaPTPAaseKFDPAPAPHQAASra 95

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1955810733  713 PFPTIASSSAQPGEQTVGLVFNQETGQWERVYRQATSSRSADAPPEALSQEMP 765
Cdd:PHA03269    96 PDPAVAPQLAAAPKPDAAEAFTSAAQAHEAPADAGTSAASKKPDPAAHTQHSP 148
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 310-422 2.04e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733  310 SPSLGESPSTSRPVVHPELPQVASQPAPHASTFSartEPRQPSEPTGAQQRPSAfttvyySAGSSLHRAVPTTHVASQPL 389
Cdd:PRK10263   746 TPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQ---QPQQPVAPQPQYQQPQQ------PVAPQPQYQQPQQPVAPQPQ 816

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1955810733  390 SQQ----LLPPPTIHQHQPPSRPLPGPDWTRSLLnMR 422
Cdd:PRK10263   817 YQQpqqpVAPQPQYQQPQQPVAPQPQDTLLHPLL-MR 852
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
59-198 5.58e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 91.13  E-value: 5.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   59 LAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTipG-LVASGCLDGEVRIWDLHGGSESW-FTES 136
Cdd:COG2319    168 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPD--GkLLASGSADGTVRLWDLATGKLLRtLTGH 245

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955810733  137 NVAIASLTFHPTAQLLLIAT-NNELHFWDWSRPEPFAVVktGSETERVRLVRFDPLGHNLLTA 198
Cdd:COG2319    246 SGSVRSVAFSPDGRLLASGSaDGTVRLWDLATGELLRTL--TGHSGGVNSVAFSPDGKLLASG 306
WD40 COG2319
WD40 repeat [General function prediction only];
59-198 6.93e-19

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 90.74  E-value: 6.93e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   59 LAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTipG-LVASGCLDGEVRIWDLHGGSESW-FTES 136
Cdd:COG2319    126 VAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPD--GkLLASGSDDGTVRLWDLATGKLLRtLTGH 203

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955810733  137 NVAIASLTFHPTAQLLLIAT-NNELHFWDWSRPEPFAVVKtgSETERVRLVRFDPLGHNLLTA 198
Cdd:COG2319    204 TGAVRSVAFSPDGKLLASGSaDGTVRLWDLATGKLLRTLT--GHSGSVRSVAFSPDGRLLASG 264
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 59-198 1.43e-18

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: 87.78  E-value: 1.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   59 LAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTIPGLVASGClDGEVRIWDLHGGSES-WFTESN 137
Cdd:cd00200    141 VAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDLSTGKCLgTLRGHE 219

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955810733  138 VAIASLTFHPTAQLLLIAT-NNELHFWDWSRPEPfavVKTGSE-TERVRLVRFDPLGHNLLTA 198
Cdd:cd00200    220 NGVNSVAFSPDGYLLASGSeDGTIRVWDLRTGEC---VQTLSGhTNSVTSLAWSPDGKRLASG 279
WD40 COG2319
WD40 repeat [General function prediction only];
36-198 3.77e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.57  E-value: 3.77e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   36 KVRWMKWQSQKVELPDSPRSTFLLAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTipG-LVASG 114
Cdd:COG2319     61 LLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPD--GkTLASG 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733  115 CLDGEVRIWDLHGGSE-SWFTESNVAIASLTFHPTAQLLLIA-TNNELHFWDWSRPEPFAVVKtgSETERVRLVRFDPLG 192
Cdd:COG2319    139 SADGTVRLWDLATGKLlRTLTGHSGAVTSVAFSPDGKLLASGsDDGTVRLWDLATGKLLRTLT--GHTGAVRSVAFSPDG 216


                   ....*.
gi 1955810733  193 HNLLTA 198
Cdd:COG2319    217 KLLASG 222
WD40 COG2319
WD40 repeat [General function prediction only];
59-166 6.23e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.80  E-value: 6.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   59 LAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTiPGLVASGCLDGEVRIWDLHGGSES-WFTESN 137
Cdd:COG2319    294 VAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPD-GKTLASGSDDGTVRLWDLATGELLrTLTGHT 372

                           90       100       110
                   ....*....|....*....|....*....|
gi 1955810733  138 VAIASLTFHPTAQLLLIA-TNNELHFWDWS 166
Cdd:COG2319    373 GAVTSVAFSPDGRTLASGsADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 59-198 5.84e-14

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: 74.29  E-value: 5.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   59 LAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTIPgLVASGCLDGEVRIWDLH-GGSESWFTESN 137
Cdd:cd00200     57 VAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGR-ILSSSSRDKTIKVWDVEtGKCLTTLRGHT 135

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955810733  138 VAIASLTFHPTAQLLLIA-TNNELHFWDwsrPEPFAVVKTGS-ETERVRLVRFDPLGHNLLTA 198
Cdd:cd00200    136 DWVNSVAFSPDGTFVASSsQDGTIKLWD---LRTGKCVATLTgHTGEVNSVAFSPDGEKLLSS 195
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 59-190 3.31e-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: 68.90  E-value: 3.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   59 LAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTIPgLVASGCLDGEVRIWDLHGGSESW-FTESN 137
Cdd:cd00200     15 VAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGT-YLASGSSDKTIRLWDLETGECVRtLTGHT 93

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1955810733  138 VAIASLTFHPTAQLLLIA-TNNELHFWDWSRPEPFAVVKtgSETERVRLVRFDP 190
Cdd:cd00200     94 SYVSSVAFSPDGRILSSSsRDKTIKVWDVETGKCLTTLR--GHTDWVNSVAFSP 145
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 59-124 4.88e-11

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: 65.43  E-value: 4.88e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955810733   59 LAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTIPGLVaSGCLDGEVRIWD 124
Cdd:cd00200    225 VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLA-SGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
59-127 1.22e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 65.32  E-value: 1.22e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955810733   59 LAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTiPGLVASGCLDGEVRIWDLHG 127
Cdd:COG2319    336 VAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPD-GRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
49-198 2.58e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.08  E-value: 2.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   49 LPDSPRSTFLLAFSPDRTLMASTHVNHNIYITEVKTGKCLHSLVGHRRTPWCVTFHPTiPGLVASGCLDGEVRIWDLHGG 128
Cdd:COG2319     32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPD-GRLLASASADGTVRLWDLATG 110

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955810733  129 SE-SWFTESNVAIASLTFHPTAQLLLIATN-NELHFWDWSRPEPFAVVKtgSETERVRLVRFDPLGHNLLTA 198
Cdd:COG2319    111 LLlRTLTGHTGAVRSVAFSPDGKTLASGSAdGTVRLWDLATGKLLRTLT--GHSGAVTSVAFSPDGKLLASG 180
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 84-124 9.62e-08

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 49.62  E-value: 9.62e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1955810733    84 TGKCLHSLVGHRRTPWCVTFHPTIPgLVASGCLDGEVRIWD 124
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGK-YLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
85-124 5.80e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 47.34  E-value: 5.80e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1955810733   85 GKCLHSLVGHRRTPWCVTFHPTiPGLVASGCLDGEVRIWD 124
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPD-GKLLASGSDDGTVKVWD 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 87-198 2.24e-06

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: 51.18  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733   87 CLHSLVGHRRTPWCVTFHPtIPGLVASGCLDGEVRIWDLHGGS-ESWFTESNVAIASLTFHPTAQLLLIA-TNNELHFWD 164
Cdd:cd00200      1 LRRTLKGHTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGElLRTLKGHTGPVRDVAASADGTYLASGsSDKTIRLWD 79

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1955810733  165 WSRPEPFAVVKtgSETERVRLVRFDPLGHNLLTA 198
Cdd:cd00200     80 LETGECVRTLT--GHTSYVSSVAFSPDGRILSSS 111
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 641-765 1.13e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.56  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733  641 RTSPASSTSAVSTQEGSSSPWRQPPSPAYEEPHASSRSRDPHPHPQERERRVAQP---PEPS---ELQPSPGPHVAAM-- 712
Cdd:PHA03269    16 NLIIANLNTNIPIPELHTSAATQKPDPAPAPHQAASRAPDPAVAPTSAASRKPDLaqaPTPAaseKFDPAPAPHQAASra 95

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1955810733  713 PFPTIASSSAQPGEQTVGLVFNQETGQWERVYRQATSSRSADAPPEALSQEMP 765
Cdd:PHA03269    96 PDPAVAPQLAAAPKPDAAEAFTSAAQAHEAPADAGTSAASKKPDPAAHTQHSP 148
PHA03247 PHA03247
large tegument protein UL36; Provisional
 580-759 2.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733  580 DPERPGPSVSShyqpqppPPAPTENNPPPFSSAAHSSRGHLNRCRACHNLLTFNHDSQRwERTSPASSTSAVSTQEGSSS 659
Cdd:PHA03247  2607 DPRGPAPPSPL-------PPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAP-GRVSRPRRARRLGRAAQASS 2678

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733  660 PWRQPPSPAYEEPHASSRSRdPHPHPQERERRVAQPPEPSELQPSPGPHVAAMPFPTIASSSAQPGEQTVGLVfnqETGQ 739
Cdd:PHA03247  2679 PPQRPRRRAARPTVGSLTSL-ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPAT---PGGP 2754

                          170       180
                   ....*....|....*....|
gi 1955810733  740 WERVYRQATSSRSADAPPEA 759
Cdd:PHA03247  2755 ARPARPPTTAGPPAPAPPAA 2774
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 310-422 2.04e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955810733  310 SPSLGESPSTSRPVVHPELPQVASQPAPHASTFSartEPRQPSEPTGAQQRPSAfttvyySAGSSLHRAVPTTHVASQPL 389
Cdd:PRK10263   746 TPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQ---QPQQPVAPQPQYQQPQQ------PVAPQPQYQQPQQPVAPQPQ 816

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1955810733  390 SQQ----LLPPPTIHQHQPPSRPLPGPDWTRSLLnMR 422
Cdd:PRK10263   817 YQQpqqpVAPQPQYQQPQQPVAPQPQDTLLHPLL-MR 852
 
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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