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Conserved domains on  [gi|19921622|ref|NP_610100|]
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Autophagy-related 18b, isoform A [Drosophila melanogaster]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 11455410)

WD40 repeat domain-containing protein similar to proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly

CATH:  2.130.10.10
PubMed:  10322433|8090199
SCOP:  4002744

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
149-251 8.87e-14

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 72.64  E-value: 8.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 149 GELRIFNASKLRTGMTIRAHDTSLSALAFSPSGALLATASERGTViRVFCVKNGQRVQEFRRGVSCVRiaSLVFSASGDF 228
Cdd:COG2319 142 GTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTV-RLWDLATGKLLRTLTGHTGAVR--SVAFSPDGKL 218

                        90       100
                ....*....|....*....|...
gi 19921622 229 LCASSNTETVHVFKIDTRAVETV 251
Cdd:COG2319 219 LASGSADGTVRLWDLATGKLLRT 241
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
149-251 8.87e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 72.64  E-value: 8.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 149 GELRIFNASKLRTGMTIRAHDTSLSALAFSPSGALLATASERGTViRVFCVKNGQRVQEFRRGVSCVRiaSLVFSASGDF 228
Cdd:COG2319 142 GTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTV-RLWDLATGKLLRTLTGHTGAVR--SVAFSPDGKL 218

                        90       100
                ....*....|....*....|...
gi 19921622 229 LCASSNTETVHVFKIDTRAVETV 251
Cdd:COG2319 219 LASGSADGTVRLWDLATGKLLRT 241
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 89-242 1.64e-09

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: 58.89  E-value: 1.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622  89 ILCVRMNRQRLIV---CLAESIHIHDIRDMKILHSIE----NIapneQGLCALSLNSHLAfpVCQTSGELRIFNASKLRT 161
Cdd:cd00200 138 VNSVAFSPDGTFVassSQDGTIKLWDLRTGKCVATLTghtgEV----NSVAFSPDGEKLL--SSSSDGTIKLWDLSTGKC 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 162 GMTIRAHDTSLSALAFSPSGALLATASERGTvIRVFCVKNGQRVQEFRR---GVSCVRiaslvFSASGDFLCASSNTETV 238
Cdd:cd00200 212 LGTLRGHENGVNSVAFSPDGYLLASGSEDGT-IRVWDLRTGECVQTLSGhtnSVTSLA-----WSPDGKRLASGSADGTI 285


                ....
gi 19921622 239 HVFK 242
Cdd:cd00200 286 RIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 163-197 2.35e-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: 2.35e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 19921622    163 MTIRAHDTSLSALAFSPSGALLATASERGTvIRVF 197
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGT-IKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
163-197 5.45e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.63  E-value: 5.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19921622   163 MTIRAHDTSLSALAFSPSGALLATASERGTvIRVF 197
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGT-VKVW 38
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
149-251 8.87e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 72.64  E-value: 8.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 149 GELRIFNASKLRTGMTIRAHDTSLSALAFSPSGALLATASERGTViRVFCVKNGQRVQEFRRGVSCVRiaSLVFSASGDF 228
Cdd:COG2319 142 GTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTV-RLWDLATGKLLRTLTGHTGAVR--SVAFSPDGKL 218

                        90       100
                ....*....|....*....|...
gi 19921622 229 LCASSNTETVHVFKIDTRAVETV 251
Cdd:COG2319 219 LASGSADGTVRLWDLATGKLLRT 241
WD40 COG2319
WD40 repeat [General function prediction only];
149-248 3.84e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 70.71  E-value: 3.84e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 149 GELRIFNASKLRTGMTIRAHDTSLSALAFSPSGALLATASERGTViRVFCVKNGQRVQEFRRGVScvRIASLVFSASGDF 228
Cdd:COG2319 226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV-RLWDLATGELLRTLTGHSG--GVNSVAFSPDGKL 302

                        90       100
                ....*....|....*....|
gi 19921622 229 LCASSNTETVHVFKIDTRAV 248
Cdd:COG2319 303 LASGSDDGTVRLWDLATGKL 322
WD40 COG2319
WD40 repeat [General function prediction only];
149-245 2.48e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 68.40  E-value: 2.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 149 GELRIFNASKLRTGMTIRAHDTSLSALAFSPSGALLATASERGTViRVFCVKNGQRVQEFRRGVScvRIASLVFSASGDF 228
Cdd:COG2319 310 GTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTV-RLWDLATGELLRTLTGHTG--AVTSVAFSPDGRT 386

                        90
                ....*....|....*..
gi 19921622 229 LCASSNTETVHVFKIDT 245
Cdd:COG2319 387 LASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
149-246 6.33e-12

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 67.24  E-value: 6.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 149 GELRIFNASKLRTGMTIRAHDTSLSALAFSPSGALLATASERGTViRVFCVKNGQRVQEFRRGVSCVRiaSLVFSASGDF 228
Cdd:COG2319 268 GTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTV-RLWDLATGKLLRTLTGHTGAVR--SVAFSPDGKT 344

                        90
                ....*....|....*...
gi 19921622 229 LCASSNTETVHVFKIDTR 246
Cdd:COG2319 345 LASGSDDGTVRLWDLATG 362
WD40 COG2319
WD40 repeat [General function prediction only];
149-245 1.58e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 62.62  E-value: 1.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 149 GELRIFNASKLRTGMTIRAHDTSLSALAFSPSGALLATASERGTViRVFCVKNGQRVQEFRRGVSCVRiaSLVFSASGDF 228
Cdd:COG2319 100 GTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTV-RLWDLATGKLLRTLTGHSGAVT--SVAFSPDGKL 176

                        90
                ....*....|....*..
gi 19921622 229 LCASSNTETVHVFKIDT 245
Cdd:COG2319 177 LASGSDDGTVRLWDLAT 193
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 89-242 1.64e-09

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: 58.89  E-value: 1.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622  89 ILCVRMNRQRLIV---CLAESIHIHDIRDMKILHSIE----NIapneQGLCALSLNSHLAfpVCQTSGELRIFNASKLRT 161
Cdd:cd00200 138 VNSVAFSPDGTFVassSQDGTIKLWDLRTGKCVATLTghtgEV----NSVAFSPDGEKLL--SSSSDGTIKLWDLSTGKC 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 162 GMTIRAHDTSLSALAFSPSGALLATASERGTvIRVFCVKNGQRVQEFRR---GVSCVRiaslvFSASGDFLCASSNTETV 238
Cdd:cd00200 212 LGTLRGHENGVNSVAFSPDGYLLASGSEDGT-IRVWDLRTGECVQTLSGhtnSVTSLA-----WSPDGKRLASGSADGTI 285


                ....
gi 19921622 239 HVFK 242
Cdd:cd00200 286 RIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 151-245 1.52e-08

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: 55.80  E-value: 1.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 151 LRIFNASKLRTGMTIRAHDTSLSALAFSPSGALLATASERGTvIRVFCVKNGQRVQEFR---RGVSCVRiaslvFSASGD 227
Cdd:cd00200  75 IRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKT-IKVWDVETGKCLTTLRghtDWVNSVA-----FSPDGT 148

                        90
                ....*....|....*...
gi 19921622 228 FLCASSNTETVHVFKIDT 245
Cdd:cd00200 149 FVASSSQDGTIKLWDLRT 166
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 132-245 4.63e-08

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: 54.26  E-value: 4.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 132 CALSLNSHLAFpVCQTSGELRIFNASKLRTGMTIRAHDTSLSALAFSPSGALLATASERGTvIRVFCVKNGQRVQEFRRG 211
Cdd:cd00200  99 VAFSPDGRILS-SSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT-IKLWDLRTGKCVATLTGH 176

                        90       100       110
                ....*....|....*....|....*....|....
gi 19921622 212 VSCVRiaSLVFSASGDFLCASSNTETVHVFKIDT 245
Cdd:cd00200 177 TGEVN--SVAFSPDGEKLLSSSSDGTIKLWDLST 208
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 164-248 7.09e-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: 47.71  E-value: 7.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 164 TIRAHDTSLSALAFSPSGALLATASERGTvIRVFCVKNGQRVQEFRRGVSCVRiaSLVFSASGDFLCASSNTETVHVFKI 243
Cdd:cd00200   4 TLKGHTGGVTCVAFSPDGKLLATGSGDGT-IKVWDLETGELLRTLKGHTGPVR--DVAASADGTYLASGSSDKTIRLWDL 80


                ....*
gi 19921622 244 DTRAV 248
Cdd:cd00200  81 ETGEC 85
WD40 COG2319
WD40 repeat [General function prediction only];
164-245 1.77e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.83  E-value: 1.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 164 TIRAHDTSLSALAFSPSGALLATASERGTViRVFCVKNGQRVQEFRRGVScvRIASLVFSASGDFLCASSNTETVHVFKI 243
Cdd:COG2319  73 TLLGHTAAVLSVAFSPDGRLLASASADGTV-RLWDLATGLLLRTLTGHTG--AVRSVAFSPDGKTLASGSADGTVRLWDL 149


                ..
gi 19921622 244 DT 245
Cdd:COG2319 150 AT 151
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 149-245 4.00e-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: 45.40  E-value: 4.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 149 GELRIFNASKLRTGMTIRAHDTSLSALAFSPSGALLATASERGTvIRVFCVKNGQRVQEFrRGVSCvRIASLVFSASGDF 228
Cdd:cd00200  31 GTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKT-IRLWDLETGECVRTL-TGHTS-YVSSVAFSPDGRI 107

                        90
                ....*....|....*..
gi 19921622 229 LCASSNTETVHVFKIDT 245
Cdd:cd00200 108 LSSSSRDKTIKVWDVET 124
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
136-252 1.59e-03

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 40.06  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921622 136 LNSHLAFPVCQTSGELRIFNASKLRTGMTIRAhDTSLSALAFSPSGALLATASERGTVIRVFCVKNGQRVQEFRRGVSCV 215
Cdd:COG3391  77 ADGRRLYVANSGSGRVSVIDLATGKVVATIPV-GGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGAGPH 155

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19921622 216 RIAslvFSASGDFL---CASSNTETVHVFKIDTRAVETVE 252
Cdd:COG3391 156 GIA---VDPDGKRLyvaNSGSNTVSVIVSVIDTATGKVVA 192
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 163-197 2.35e-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: 2.35e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 19921622    163 MTIRAHDTSLSALAFSPSGALLATASERGTvIRVF 197
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGT-IKLW 39
WD40 pfam00400
WD domain, G-beta repeat;
163-197 5.45e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 34.63  E-value: 5.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 19921622   163 MTIRAHDTSLSALAFSPSGALLATASERGTvIRVF 197
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGT-VKVW 38
 
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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