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Conserved domains on  [gi|767918207|ref|XP_011509510|]
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astacin-like metalloendopeptidase isoform X3 [Homo sapiens]

Protein Classification

zinc metalloprotease( domain architecture ID 1881)

zinc metalloprotease may be a member of the astacin-like protease family or the adamalysin/reprolysin-like protease family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 105-245 2.75e-70

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.


The actual alignment was detected with superfamily member cd04283:

Pssm-ID: 469599 [Multi-domain]  Cd Length: 182  Bit Score: 213.66  E-value: 2.75e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207 105 GVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSL-APTCLQKGrg 183
Cdd:cd04283    2 GIVYVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLqKQGCMYKG-- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767918207 184 IVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSSNMLTPYDYSSVMHYGR 245
Cdd:cd04283   80 IIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLGTPYDYSSVMHYGR 141
 
Name Accession Description Interval E-value
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 105-245 2.75e-70

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: 213.66  E-value: 2.75e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207 105 GVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSL-APTCLQKGrg 183
Cdd:cd04283    2 GIVYVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLqKQGCMYKG-- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767918207 184 IVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSSNMLTPYDYSSVMHYGR 245
Cdd:cd04283   80 IIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLGTPYDYSSVMHYGR 141
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 97-245 1.61e-56

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: 179.01  E-value: 1.61e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207   97 NKWPMGgsgvvEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQ--RDFISIIPMYGCFSSVGRSGGMQVVSLA 174
Cdd:pfam01400   1 KKWPNG-----PIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApdNNYLFFFKGDGCYSYVGRVGGRQPVSIG 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767918207  175 PTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIK---SQSSNMLTPYDYSSVMHYGR 245
Cdd:pfam01400  76 DGCDKFG--IIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKydpSEVDSYGVPYDYGSIMHYGP 147
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 96-239 1.20e-38

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: 131.32  E-value: 1.20e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207    96 SNKWPmggsgVVEVPF-LLSSKYDEPSRQVILEALAEFERSTCIRFV-TYQDQRDFISIIPMY-GCF-SSVGRSGGMQVV 171
Cdd:smart00235   2 SKKWP-----KGTVPYvIDSSSLSPEEREAIAKALAEWSDVTCIRFVeRTGTADIYISFGSGDsGCTlSHAGRPGGDQHL 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767918207   172 SLAPTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGfeiNFIKSQSSNMLTPYDYSS 239
Cdd:smart00235  77 SLGNGCINTG--VAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDDSLGIPYDYGS 139
 
Name Accession Description Interval E-value
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
 105-245 2.75e-70

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: 213.66  E-value: 2.75e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207 105 GVVEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSL-APTCLQKGrg 183
Cdd:cd04283    2 GIVYVPYVISPQYSENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVSLqKQGCMYKG-- 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767918207 184 IVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSSNMLTPYDYSSVMHYGR 245
Cdd:cd04283   80 IIQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLGTPYDYSSVMHYGR 141
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
 109-245 1.93e-68

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: 208.96  E-value: 1.93e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207 109 VPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSLAPTCLQKgrGIVLHE 188
Cdd:cd04280    4 VPYVIDGSFDESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCFSL--GTIVHE 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207 189 LMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIK---SQSSNMLTPYDYSSVMHYGR 245
Cdd:cd04280   82 LMHALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDKyspDTVTTYGVPYDYGSVMHYGP 141
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 97-245 1.61e-56

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: 179.01  E-value: 1.61e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207   97 NKWPMGgsgvvEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQ--RDFISIIPMYGCFSSVGRSGGMQVVSLA 174
Cdd:pfam01400   1 KKWPNG-----PIPYVIDGSLTGLARALIRQAMRHWENKTCIRFVERTPApdNNYLFFFKGDGCYSYVGRVGGRQPVSIG 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767918207  175 PTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIK---SQSSNMLTPYDYSSVMHYGR 245
Cdd:pfam01400  76 DGCDKFG--IIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKydpSEVDSYGVPYDYGSIMHYGP 147
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
 57-244 4.48e-42

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: 143.38  E-value: 4.48e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207  57 DKDIPAINQGLILEetpessfLIEGDI-IRPSPFRL-LSATSNKWPMggsgvvEVPFLLSSKYDEPSRQVILEALAEFER 134
Cdd:cd04282    9 DQDIFEINLGAGLD-------LFEGDIlLDEGQSRNgLIGDTYRWPF------PIPYILDDSLDLNAKGVILKAFEMYRL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207 135 STCIRFVTYQDQRDFISIIPMYGCFSSVGRSGGMQVVSLAPTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNE 214
Cdd:cd04282   76 KSCVDFKPYEGESNYIFFFKGSGCWSMVGDQQGGQNLSIGAGCDYKA--TVEHEFLHALGFYHEQSRSDRDDYVKIWWDQ 153

                        170       180       190
                 ....*....|....*....|....*....|...
gi 767918207 215 ILPGFEINFIK---SQSSNMLTPYDYSSVMHYG 244
Cdd:cd04282  154 ILSGREHNFNKyddSFSTDLNTPYDYESVMHYS 186
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 96-239 1.20e-38

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: 131.32  E-value: 1.20e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207    96 SNKWPmggsgVVEVPF-LLSSKYDEPSRQVILEALAEFERSTCIRFV-TYQDQRDFISIIPMY-GCF-SSVGRSGGMQVV 171
Cdd:smart00235   2 SKKWP-----KGTVPYvIDSSSLSPEEREAIAKALAEWSDVTCIRFVeRTGTADIYISFGSGDsGCTlSHAGRPGGDQHL 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767918207   172 SLAPTCLQKGrgIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGfeiNFIKSQSSNMLTPYDYSS 239
Cdd:smart00235  77 SLGNGCINTG--VAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDDSLGIPYDYGS 139
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
 93-245 4.99e-37

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: 129.10  E-value: 4.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207  93 SATSNKWPmggSGVVevPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRDFISI-IPMYGCFSSVGRSG-GMQV 170
Cdd:cd04281    4 ARKERIWP---GGVI--PYVIDGNFTGSQRAMFKQAMRHWENFTCVTFVERTPEENYIVFtYRPCGCCSYVGRRGnGPQA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767918207 171 VSLAPTClqKGRGIVLHELMHVLGFWHEHTRADRDRYIRVNWNEILPGFEINFIKSQSS---NMLTPYDYSSVMHYGR 245
Cdd:cd04281   79 ISIGKNC--DKFGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFLKMEPEevdSLGEPYDFDSIMHYAR 154
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 107-244 1.80e-15

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: 71.78  E-value: 1.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207 107 VEVPFLL--------SSKYDEPSRQVILEALAEFERSTCIRFV--TYQDQRDFIsIIPMY--------GCFSSVGRS--G 166
Cdd:cd00203    1 KVIPYVVvaddrdveEENLSAQIQSLILIAMQIWRDYLNIRFVlvGVEIDKADI-AILVTrqdfdggtGGWAYLGRVcdS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207 167 GMQVVSLAPTCLQK--GRGIVLHELMHVLGFWHEHTRADRDRYIRVNwneilpgfeinfiksqSSNMLTPYDYSSVMHYG 244
Cdd:cd00203   80 LRGVGVLQDNQSGTkeGAQTIAHELGHALGFYHDHDRKDRDDYPTID----------------DTLNAEDDDYYSVMSYT 143
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 108-247 6.68e-15

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: 70.22  E-value: 6.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207 108 EVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTYQDQRD------FISIIPMY-GCFSSVGRSGGM--QVVSLAPTCL 178
Cdd:cd04268    3 PITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKNANDVDPadirysVIRWIPYNdGTWSYGPSQVDPltGEILLARVYL 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767918207 179 QKG---------RGIVLHELMHVLGFWHEHTRADRDRYIRVNwneilpgfeinfiksqssnmLTPYDYSSVMHYGRVP 247
Cdd:cd04268   83 YSSfveysgarlRNTAEHELGHALGLRHNFAASDRDDNVDLL--------------------AEKGDTSSVMDYAPSN 140
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 98-243 5.46e-06

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 45.83  E-value: 5.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207  98 KWPMGGsgVVEVPFLLSSkyDEPSRQVILEALAEFER--STCIRFVTYQDQRDFISIIPMYGCFSSVGRSGgMQVVSLAP 175
Cdd:cd04327    2 LWRNGT--VLRIAFLGGP--DAFLKDKVRAAAREWLPyaNLKFKFVTDADADIRISFTPGDGYWSYVGTDA-LLIGADAP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207 176 T----------CLQKGRGIVLHELMHVLGFWHEHTRAD----------RDRYIR--VNWNEILPgfEINFIKSQSSNML- 232
Cdd:cd04327   77 TmnlgwftddtPDPEFSRVVLHEFGHALGFIHEHQSPAanipwdkeavYAYFSGppNWDRETVI--NHNVFAKLDDGDVa 154

                        170
                 ....*....|..
gi 767918207 233 -TPYDYSSVMHY 243
Cdd:cd04327  155 ySPYDPDSIMHY 166
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 107-201 2.14e-04

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 40.52  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767918207 107 VEVPFLLSSKYDEPSRQVILEALAEFERSTCIRFVTY--QDQRDFISI--------------IPMYG-CFSSVGRSGGMQ 169
Cdd:cd04279    8 IDPTPAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNpeEDNDADIVIffdrpppvggagggLARAGfPLISDGNRKLFN 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767918207 170 VVSLA--------PTCLQkgrGIVLHELMHVLGFWHEHTR 201
Cdd:cd04279   88 RTDINlgpgqprgAENLQ---AIALHELGHALGLWHHSDR 124
 
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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