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Conserved domains on  [gi|488933978|ref|WP_002845053|]
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metallophosphoesterase family protein [Peptostreptococcus anaerobius]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10582454)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

CATH:  3.60.21.10
Gene Ontology:  GO:0046872|GO:0042578
PubMed:  25837850
SCOP:  3001067

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
1-149 1.50e-33

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


:

Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 115.49  E-value: 1.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978    1 MKLLILSDSHHSIDRLNKLLpIIEEEKIDIIVHAGDNFRDSVYLKEKSKKPVIGVIGNCDFENTDR-----EIEFELEGL 75
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAAL-ERLKGVVDLIIHAGDIVAPEVLEELLELAPVLAVRGNNDAAAEFAtdlpeEAVLELGGV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488933978   76 KFFLTHGHRYSVKYGPEILASKGqeiGANIVVYGHTHIKDDTYMGGLLILNPGSLSQPRDGSRGSYVVMDVDNG 149
Cdd:pfam12850  80 KILLTHGHGVKDALARLLRRAEE---GVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDIDDG 150
 
Name Accession Description Interval E-value
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
1-149 1.50e-33

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 115.49  E-value: 1.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978    1 MKLLILSDSHHSIDRLNKLLpIIEEEKIDIIVHAGDNFRDSVYLKEKSKKPVIGVIGNCDFENTDR-----EIEFELEGL 75
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAAL-ERLKGVVDLIIHAGDIVAPEVLEELLELAPVLAVRGNNDAAAEFAtdlpeEAVLELGGV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488933978   76 KFFLTHGHRYSVKYGPEILASKGqeiGANIVVYGHTHIKDDTYMGGLLILNPGSLSQPRDGSRGSYVVMDVDNG 149
Cdd:pfam12850  80 KILLTHGHGVKDALARLLRRAEE---GVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDIDDG 150
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
2-153 4.70e-32

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 111.98  E-value: 4.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978   2 KLLILSDSHHSIDRLNKLLpIIEEEKIDIIVHAGDNFRDSVYLKEKSKK-PVIGVIGNCDFE--------NTDREIEFEL 72
Cdd:cd00841    1 KIGVISDTHGNLEAIEKAL-ELFEDGVDAVIHAGDFVSPFVLNALLELKaPLIAVRGNNDGEvdqllgrpILPEFLTLEI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978  73 EGLKFFLTHGHRYSVKYgpeiLASKGQEIGANIVVYGHTHIKDDTYMGGLLILNPGSLSQPRdGSRGSYVVMDVDNGSYQ 152
Cdd:cd00841   80 GGLRILLTHGHLFGVLE----ALYLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPR-GGRPTYAILDIEKLEVE 154

                 .
gi 488933978 153 Y 153
Cdd:cd00841  155 I 155
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-152 1.71e-31

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 111.16  E-value: 1.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978   2 KLLILSDSHHSIDRLNKLLPIIEEEKIDIIVHAGDnfrdSVYLKEKS--------KKPVIGVIGNCDFENTD------RE 67
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEDLEREGVDLIVHLGD----LVGYGPDPpevldllrELPIVAVRGNHDGAVLRglrslpET 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978  68 IEFELEGLKFFLTHGHRYSVKYGP---EILASKGQEIGANIVVYGHTHIKDDTYMGGLLILNPGSLSQPRDGSRGSYVVM 144
Cdd:COG0622   77 LRLELEGVRILLVHGSPNEYLLPDtpaERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDGDPASYAIL 156

                 ....*...
gi 488933978 145 DVDNGSYQ 152
Cdd:COG0622  157 DIDDGEWS 164
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
1-151 3.18e-25

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 94.36  E-value: 3.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978    1 MKLLILSDSH---HSIDRLNKLLpiIEEEKIDIIVHAGDnFRDSVYLKEKSK--KPVIGVIGNCDFE--NTDREIEFELE 73
Cdd:TIGR00040   1 MKILVISDTHgplRATELPVELF--NLESNVDLVIHAGD-LTSPFVLKEFEDlaAKVIAVRGNNDGErdELPEEEIFEAE 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488933978   74 GLKFFLTHGHRYSVKYGPEILASKGQEIGANIVVYGHTHIKDDTYMGGLLILNPGSLSQPRDGSRGSYVVMDVDNGSY 151
Cdd:TIGR00040  78 GIDFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSYAILDVDKDKV 155
PRK09453 PRK09453
phosphodiesterase; Provisional
1-147 2.82e-22

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 87.23  E-value: 2.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978   1 MKLLILSDSHHSIDRLNKLLPIIEEEKIDIIVHAGD--------------NFRDSVYLKEKSKKPVIGVIGNCDFENTDR 66
Cdd:PRK09453   1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDvlyhgprnplpegyAPKKVAELLNAYADKIIAVRGNCDSEVDQM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978  67 EIEF---------ELEGLKFFLTHGHRYSvkygPEILASKGQeigANIVVYGHTHIKDDTYMGGLLILNPGSLSQPRDGS 137
Cdd:PRK09453  81 LLHFpimapyqqvLLEGKRLFLTHGHLYG----PENLPALHD---GDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGGY 153
                        170
                 ....*....|
gi 488933978 138 RGSYVVMDVD 147
Cdd:PRK09453 154 PASYGILDDN 163
 
Name Accession Description Interval E-value
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
1-149 1.50e-33

Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the Calcineurin-like phosphoesterase superfamily.


Pssm-ID: 432832 [Multi-domain]  Cd Length: 150  Bit Score: 115.49  E-value: 1.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978    1 MKLLILSDSHHSIDRLNKLLpIIEEEKIDIIVHAGDNFRDSVYLKEKSKKPVIGVIGNCDFENTDR-----EIEFELEGL 75
Cdd:pfam12850   1 MRIGIISDTHDNLALPEAAL-ERLKGVVDLIIHAGDIVAPEVLEELLELAPVLAVRGNNDAAAEFAtdlpeEAVLELGGV 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488933978   76 KFFLTHGHRYSVKYGPEILASKGqeiGANIVVYGHTHIKDDTYMGGLLILNPGSLSQPRDGSRGSYVVMDVDNG 149
Cdd:pfam12850  80 KILLTHGHGVKDALARLLRRAEE---GVAVVVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDIDDG 150
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
2-153 4.70e-32

Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a manganase-dependent metallophosphatase, found in bacteria and archaea, that cleaves bis-p-nitrophenyl phosphate, thymidine 5'-monophosphate-p-nitrophenyl ester, and p-nitrophenyl phosphorylcholine, but is unable to hydrolyze 2',3 ' or 3',5' cyclic nucleic phosphodiesters, and various phosphomonoesters, including p-nitrophenyl phosphate. This family also includes the Bacilus subtilis YsnB and Methanococcus jannaschii MJ0936 proteins. This domain family belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277320 [Multi-domain]  Cd Length: 156  Bit Score: 111.98  E-value: 4.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978   2 KLLILSDSHHSIDRLNKLLpIIEEEKIDIIVHAGDNFRDSVYLKEKSKK-PVIGVIGNCDFE--------NTDREIEFEL 72
Cdd:cd00841    1 KIGVISDTHGNLEAIEKAL-ELFEDGVDAVIHAGDFVSPFVLNALLELKaPLIAVRGNNDGEvdqllgrpILPEFLTLEI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978  73 EGLKFFLTHGHRYSVKYgpeiLASKGQEIGANIVVYGHTHIKDDTYMGGLLILNPGSLSQPRdGSRGSYVVMDVDNGSYQ 152
Cdd:cd00841   80 GGLRILLTHGHLFGVLE----ALYLAKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPR-GGRPTYAILDIEKLEVE 154

                 .
gi 488933978 153 Y 153
Cdd:cd00841  155 I 155
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
2-152 1.71e-31

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 111.16  E-value: 1.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978   2 KLLILSDSHHSIDRLNKLLPIIEEEKIDIIVHAGDnfrdSVYLKEKS--------KKPVIGVIGNCDFENTD------RE 67
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEDLEREGVDLIVHLGD----LVGYGPDPpevldllrELPIVAVRGNHDGAVLRglrslpET 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978  68 IEFELEGLKFFLTHGHRYSVKYGP---EILASKGQEIGANIVVYGHTHIKDDTYMGGLLILNPGSLSQPRDGSRGSYVVM 144
Cdd:COG0622   77 LRLELEGVRILLVHGSPNEYLLPDtpaERLRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDGDPASYAIL 156

                 ....*...
gi 488933978 145 DVDNGSYQ 152
Cdd:COG0622  157 DIDDGEWS 164
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
1-151 3.18e-25

phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif approximating DXH(X25)GDXXD(X25)GNHD as found in several phosphoesterases, including the nucleases SbcD and Mre11, and a family of uncharacterized archaeal putative phosphoesterases described by TIGR00024. In this family, the His residue in GNHD portion of the motif is not conserved. The member MJ0936, one of two from Methanococcus jannaschii, was shown () to act on model phosphodiesterase substrates; a divalent cation was required. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272869 [Multi-domain]  Cd Length: 158  Bit Score: 94.36  E-value: 3.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978    1 MKLLILSDSH---HSIDRLNKLLpiIEEEKIDIIVHAGDnFRDSVYLKEKSK--KPVIGVIGNCDFE--NTDREIEFELE 73
Cdd:TIGR00040   1 MKILVISDTHgplRATELPVELF--NLESNVDLVIHAGD-LTSPFVLKEFEDlaAKVIAVRGNNDGErdELPEEEIFEAE 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488933978   74 GLKFFLTHGHRYSVKYGPEILASKGQEIGANIVVYGHTHIKDDTYMGGLLILNPGSLSQPRDGSRGSYVVMDVDNGSY 151
Cdd:TIGR00040  78 GIDFGLVHGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSYAILDVDKDKV 155
PRK09453 PRK09453
phosphodiesterase; Provisional
1-147 2.82e-22

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 87.23  E-value: 2.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978   1 MKLLILSDSHHSIDRLNKLLPIIEEEKIDIIVHAGD--------------NFRDSVYLKEKSKKPVIGVIGNCDFENTDR 66
Cdd:PRK09453   1 MKLMFASDTHGSLPATEKALELFAQSGADWLVHLGDvlyhgprnplpegyAPKKVAELLNAYADKIIAVRGNCDSEVDQM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978  67 EIEF---------ELEGLKFFLTHGHRYSvkygPEILASKGQeigANIVVYGHTHIKDDTYMGGLLILNPGSLSQPRDGS 137
Cdd:PRK09453  81 LLHFpimapyqqvLLEGKRLFLTHGHLYG----PENLPALHD---GDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGGY 153
                        170
                 ....*....|
gi 488933978 138 RGSYVVMDVD 147
Cdd:PRK09453 154 PASYGILDDN 163
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
2-150 3.06e-08

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 50.78  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978   2 KLLILSDSHHSIDRLNKLLPIIEEEKIDIIVHAGD--NFRDSVYLKE------KSKKPVIGVIGNCDFENTDREIE---- 69
Cdd:COG2129    1 KILAVSDLHGNFDLLEKLLELARAEDADLVILAGDltDFGTAEEAREvleelaALGVPVLAVPGNHDDPEVLDALEesgv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978  70 -------FELEGLKF------------------------------------FLTH----GHRYSVKYGPEILASKG---- 98
Cdd:COG2129   81 hnlhgrvVEIGGLRIaglggsrptpfgtpyeyteeeieerlaklrekdvdiLLTHappyGTTLDRVEDGPHVGSKAlrel 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488933978  99 -QEIGANIVVYGHTHI-KDDTYMGGLLILNPGSLsqprdgSRGSYVVMDVDNGS 150
Cdd:COG2129  161 iEEFQPKLVLHGHIHEsRGVDKIGGTRVVNPGSL------AEGYYALIDLEDRS 208
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
4-128 2.50e-06

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 44.18  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488933978   4 LILSDSHHSIDRLNKLLPIIEEEKIDII--VHAGDNF---------RDSVYLKEKSKKPVIGVIGNCDfentdreiefel 72
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAALAKAEKPDlvICLGDLVdygpdpeevELKALRLLLAGIPVYVVPGNHD------------ 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488933978  73 eglkFFLTHGHRYSVK--------YGPEILASKGQEIGANIVVYGHTHIKDDTYM--GGLLILNPG 128
Cdd:cd00838   69 ----ILVTHGPPYDPLdegspgedPGSEALLELLDKYGPDLVLSGHTHVPGRREVdkGGTLVVNPG 130
 
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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