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Conserved domains on  [gi|157831414|pdb|1IAB|A]
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Chain A, ASTACIN

Protein Classification

M12 family metallopeptidase( domain architecture ID 10136691)

M12 family metallopeptidase such as astacin, a digestive enzyme isolated from crayfish, belongs to a group of zinc-dependent proteolytic enzymes with an HExxH zinc-binding site/active site

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 12-194 2.17e-78

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. This family includes: astacin, a digestive enzyme from Crayfish; meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain, proteins involved in (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


:

Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 232.08  E-value: 2.17e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       12 GGVIPYTFAG-VSGADQSAILSGMQELEEKTCIRFVPRTTESDYVEIFtSGSGCWSYVGRISGAQQVSLQaNGCVYHGTI 90
Cdd:cd04280   1 NGTVPYVIDGsFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIV-KGSGCWSYVGRVGGRQVVSLG-SGCFSLGTI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       91 IHELMHAIGFYHEHTRMDRDNYVTINYQNVDPSMTSNFDIDTYSR--YVGEDYQYYSIMHYGKYSFSIqwGVLETIVPLQ 168
Cdd:cd04280  79 VHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTvtTYGVPYDYGSVMHYGPTAFSK--NGKPTIVPKD 156

                       170       180
                ....*....|....*....|....*.
1IAB_A      169 NGIDLTdpYDKAHMLQTDANQINNLY 194
Cdd:cd04280 157 PGYQII--GQREGLSFLDIKKINKMY 180
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 12-194 2.17e-78

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. This family includes: astacin, a digestive enzyme from Crayfish; meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain, proteins involved in (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 232.08  E-value: 2.17e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       12 GGVIPYTFAG-VSGADQSAILSGMQELEEKTCIRFVPRTTESDYVEIFtSGSGCWSYVGRISGAQQVSLQaNGCVYHGTI 90
Cdd:cd04280   1 NGTVPYVIDGsFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIV-KGSGCWSYVGRVGGRQVVSLG-SGCFSLGTI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       91 IHELMHAIGFYHEHTRMDRDNYVTINYQNVDPSMTSNFDIDTYSR--YVGEDYQYYSIMHYGKYSFSIqwGVLETIVPLQ 168
Cdd:cd04280  79 VHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTvtTYGVPYDYGSVMHYGPTAFSK--NGKPTIVPKD 156

                       170       180
                ....*....|....*....|....*.
1IAB_A      169 NGIDLTdpYDKAHMLQTDANQINNLY 194
Cdd:cd04280 157 PGYQII--GQREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 8-194 2.35e-67

Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family contain two conserved disulphide bridges, these are joined 1-4 and 2-3. Members of this family have an amino terminal propeptide which is cleaved to give the active protease domain. All other linked domains are found to the carboxyl terminus of this domain. This family includes: Astacin, a digestive enzyme from Crayfish. Meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain. Proteins involved in morphogenesis such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 204.44  E-value: 2.35e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A          8 YLWSGGVIPYTFAG-VSGADQSAILSGMQELEEKTCIRFVPRTT--ESDYVEIFtSGSGCWSYVGRISGAQQVSLqANGC 84
Cdd:pfam01400   1 KKWPNGPIPYVIDGsLTGLARALIRQAMRHWENKTCIRFVERTPapDNNYLFFF-KGDGCYSYVGRVGGRQPVSI-GDGC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A         85 VYHGTIIHELMHAIGFYHEHTRMDRDNYVTINYQNVDPSMTSNFD------IDTYsryvGEDYQYYSIMHYGKYSFSIQW 158
Cdd:pfam01400  79 DKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDkydpseVDSY----GVPYDYGSIMHYGPNAFSKNG 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
1IAB_A        159 GvLETIVPLQNGIDLTDPyDKAHMLQTDANQINNLY 194
Cdd:pfam01400 155 S-LPTIVPKDNDYQATIG-QRVKLSFYDIKKINKLY 188
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 9-142 5.17e-43

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 140.95  E-value: 5.17e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A           9 LWSGGVIPYTFA--GVSGADQSAILSGMQELEEKTCIRFVPRT-TESDYVEIFTSGSGCW-SYVGRISGAQQVSLqANGC 84
Cdd:smart00235   4 KWPKGTVPYVIDssSLSPEEREAIAKALAEWSDVTCIRFVERTgTADIYISFGSGDSGCTlSHAGRPGGDQHLSL-GNGC 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
1IAB_A          85 VYHGTIIHELMHAIGFYHEHTRMDRDNYVTINYQNVdpsMTSNFDIDTYSRY-VGEDYQ 142
Cdd:smart00235  83 INTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNI---DTRNFDLSEDDSLgIPYDYG 138
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 12-194 2.17e-78

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. This family includes: astacin, a digestive enzyme from Crayfish; meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain, proteins involved in (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 232.08  E-value: 2.17e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       12 GGVIPYTFAG-VSGADQSAILSGMQELEEKTCIRFVPRTTESDYVEIFtSGSGCWSYVGRISGAQQVSLQaNGCVYHGTI 90
Cdd:cd04280   1 NGTVPYVIDGsFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIV-KGSGCWSYVGRVGGRQVVSLG-SGCFSLGTI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       91 IHELMHAIGFYHEHTRMDRDNYVTINYQNVDPSMTSNFDIDTYSR--YVGEDYQYYSIMHYGKYSFSIqwGVLETIVPLQ 168
Cdd:cd04280  79 VHELMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKYSPDTvtTYGVPYDYGSVMHYGPTAFSK--NGKPTIVPKD 156

                       170       180
                ....*....|....*....|....*.
1IAB_A      169 NGIDLTdpYDKAHMLQTDANQINNLY 194
Cdd:cd04280 157 PGYQII--GQREGLSFLDIKKINKMY 180
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 15-194 7.58e-68

Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted by teleost embryos to digest the egg envelope or chorion. In some teleosts, the hatching enzyme may be a system consisting of two evolutionary related metalloproteases, high choriolytic enzyme and low choriolytic enzyme (HCE and LCE), which may have different substrate specificities and cooperatively digest the chorion.


Pssm-ID: 239810 [Multi-domain]  Cd Length: 182  Bit Score: 205.57  E-value: 7.58e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       15 IPYTFAGVSGADQ-SAILSGMQELEEKTCIRFVPRTTESDYVEIfTSGSGCWSYVGRISGAQQVSLQANGCVYHGTIIHE 93
Cdd:cd04283   6 VPYVISPQYSENErAVIEKAMQEFETLTCVRFVPRTTERDYLNI-ESRSGCWSYIGRQGGRQTVSLQKQGCMYKGIIQHE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       94 LMHAIGFYHEHTRMDRDNYVTINYQNVDPSMTSNFD-IDTysRYVGEDYQYYSIMHYGKYSFSIQWgvLETIVPlqngid 172
Cdd:cd04283  85 LLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDkQDT--NNLGTPYDYSSVMHYGRYAFSING--KPTIVP------ 154

                       170       180
                ....*....|....*....|....*.
1IAB_A      173 LTDPY----DKAHMLQTDANQINNLY 194
Cdd:cd04283 155 IPDPNvpigQRQGMSNLDILRINKLY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 8-194 2.35e-67

Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family contain two conserved disulphide bridges, these are joined 1-4 and 2-3. Members of this family have an amino terminal propeptide which is cleaved to give the active protease domain. All other linked domains are found to the carboxyl terminus of this domain. This family includes: Astacin, a digestive enzyme from Crayfish. Meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain. Proteins involved in morphogenesis such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 204.44  E-value: 2.35e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A          8 YLWSGGVIPYTFAG-VSGADQSAILSGMQELEEKTCIRFVPRTT--ESDYVEIFtSGSGCWSYVGRISGAQQVSLqANGC 84
Cdd:pfam01400   1 KKWPNGPIPYVIDGsLTGLARALIRQAMRHWENKTCIRFVERTPapDNNYLFFF-KGDGCYSYVGRVGGRQPVSI-GDGC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A         85 VYHGTIIHELMHAIGFYHEHTRMDRDNYVTINYQNVDPSMTSNFD------IDTYsryvGEDYQYYSIMHYGKYSFSIQW 158
Cdd:pfam01400  79 DKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDkydpseVDSY----GVPYDYGSIMHYGPNAFSKNG 154

                         170       180       190
                  ....*....|....*....|....*....|....*.
1IAB_A        159 GvLETIVPLQNGIDLTDPyDKAHMLQTDANQINNLY 194
Cdd:pfam01400 155 S-LPTIVPKDNDYQATIG-QRVKLSFYDIKKINKLY 188
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 1-194 7.68e-49

Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) and TLD (tolloid)-like metalloproteases play vital roles in extracellular matrix formation, by cleaving precursor proteins such as enzymes, structural proteins, and proteins involved in the mineralization of the extracellular matrix. The drosophila protein tolloid and its Xenopus homologue xolloid cleave and inactivate Sog and chordin, respectively, which are inhibitors of Dpp (the Drosophila decapentaplegic gene product) and its homologue BMP4, involved in dorso-ventral patterning.


Pssm-ID: 239808 [Multi-domain]  Cd Length: 200  Bit Score: 157.60  E-value: 7.68e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A        1 AAILGDEYLWSGGVIPYTFAG-VSGADQSAILSGMQELEEKTCIRFVPRTTESDYVeIFTSGS-GCWSYVGR-ISGAQQV 77
Cdd:cd04281   1 AATARKERIWPGGVIPYVIDGnFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYI-VFTYRPcGCCSYVGRrGNGPQAI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       78 SLQANgCVYHGTIIHELMHAIGFYHEHTRMDRDNYVTINYQNVDPSMTSNFDIDTYSRY--VGEDYQYYSIMHYGKYSFS 155
Cdd:cd04281  80 SIGKN-CDKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEEVdsLGEPYDFDSIMHYARNTFS 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
1IAB_A      156 iQWGVLETIVP--LQNGIDLTDPyDKAHMLQTDANQINNLY 194
Cdd:cd04281 159 -RGMFLDTILPkrDPNGVRPEIG-QRTRLSEGDIIQANKLY 197
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 9-142 5.17e-43

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 140.95  E-value: 5.17e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A           9 LWSGGVIPYTFA--GVSGADQSAILSGMQELEEKTCIRFVPRT-TESDYVEIFTSGSGCW-SYVGRISGAQQVSLqANGC 84
Cdd:smart00235   4 KWPKGTVPYVIDssSLSPEEREAIAKALAEWSDVTCIRFVERTgTADIYISFGSGDSGCTlSHAGRPGGDQHLSL-GNGC 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
1IAB_A          85 VYHGTIIHELMHAIGFYHEHTRMDRDNYVTINYQNVdpsMTSNFDIDTYSRY-VGEDYQ 142
Cdd:smart00235  83 INTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNI---DTRNFDLSEDDSLgIPYDYG 138
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 2-154 7.62e-36

Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted extracellular proteases, which cleave a variety of targets, including peptides such as parathyroid hormone, gastrin, and cholecystokinin, cytokines such as osteopontin, and proteins such as collagen IV, fibronectin, casein and gelatin. Meprins may also be able to release proteins from the cell surface. Closely related meprin alpha- and beta-subunits form homo- and hetero-oligomers; these complexes are found on epithelial cells of the intestine, for example, and are also expressed in certain cancer cells.


Pssm-ID: 239809 [Multi-domain]  Cd Length: 230  Bit Score: 125.28  E-value: 7.62e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A        2 AILGDEYLWSGgVIPYTFAGVSGAD-QSAILSGMQELEEKTCIRFVPRTTESDYVeIFTSGSGCWSYVGRISGAQQVSLQ 80
Cdd:cd04282  38 GLIGDTYRWPF-PIPYILDDSLDLNaKGVILKAFEMYRLKSCVDFKPYEGESNYI-FFFKGSGCWSMVGDQQGGQNLSIG 115

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1IAB_A       81 ANgCVYHGTIIHELMHAIGFYHEHTRMDRDNYVTINYQNVDPSMTSNFDI--DTYSRYVGEDYQYYSIMHYGKYSF 154
Cdd:cd04282 116 AG-CDYKATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKydDSFSTDLNTPYDYESVMHYSPFSF 190
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 13-194 7.87e-33

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 115.70  E-value: 7.87e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       13 GVIPYTFAGV---------SGADQSAILSGMQELEEKTCIRFVPRTTE--SDYVEIFTS------GSGCWSYVGRI--SG 73
Cdd:cd00203   1 KVIPYVVVADdrdveeenlSAQIQSLILIAMQIWRDYLNIRFVLVGVEidKADIAILVTrqdfdgGTGGWAYLGRVcdSL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       74 AQQVSLQANGCV---YHGTIIHELMHAIGFYHEHTRMDRDNYVTInyqnvdpsmtsnfdidtYSRYVGEDYQYYSIMHYG 150
Cdd:cd00203  81 RGVGVLQDNQSGtkeGAQTIAHELGHALGFYHDHDRKDRDDYPTI-----------------DDTLNAEDDDYYSVMSYT 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
1IAB_A      151 KYSFSIqwgvletivplqngidltdpYDKAHMLQTDANQINNLY 194
Cdd:cd00203 144 KGSFSD--------------------GQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 13-194 1.42e-22

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 89.09  E-value: 1.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       13 GVIPYTFA-GVSGADQSAILSGMQELEEKTCIRFVPRTTES-DYVEIFTS-----GSGCWSYVGRISGA--QQVSLQANG 83
Cdd:cd04268   2 KPITYYIDdSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDpADIRYSVIrwipyNDGTWSYGPSQVDPltGEILLARVY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IAB_A       84 C----------VYHGTIIHELMHAIGFYHEHTRMDRDNYVTinyqnvdpsmtsnfdidtysrYVGEDYQYYSIMHYGKYS 153
Cdd:cd04268  82 LyssfveysgaRLRNTAEHELGHALGLRHNFAASDRDDNVD---------------------LLAEKGDTSSVMDYAPSN 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
1IAB_A      154 FSIQWGvletivplqngidltdPYDKAHMLQTDANQINNLY 194
Cdd:cd04268 141 FSIQLG----------------DGQKYTIGPYDIAAIKKLY 165
 
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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