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Conserved domains on  [gi|581832104|gb|EVS34461|]
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phosphodiesterase [Staphylococcus aureus M1356]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 3-146 7.54e-24

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.


The actual alignment was detected with superfamily member cd00841:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 156  Bit Score: 91.18  E-value: 7.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104   3 KWIIVSDNHTESGVLYQIYE-MHPDADVYLHLGDSEfaYDDTELSLFNR------VKGNCDF-------YPEFENEAVAK 68
Cdd:cd00841    1 KIGVISDTHGNLEAIEKALElFEDGVDAVIHAGDFV--SPFVLNALLELkapliaVRGNNDGevdqllgRPILPEFLTLE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581832104  69 YNDVKAFYTHGHLYQVNRTRDLlaekGLELGCLFAFYGHTHVAKYEYINGVHVINPGSISQSRSSmEETYAEVIIDDQ 146
Cdd:cd00841   79 IGGLRILLTHGHLFGVLEALYL----AKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGG-RPTYAILDIEKL 151
 
Name Accession Description Interval E-value
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 3-146 7.54e-24

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: 91.18  E-value: 7.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104   3 KWIIVSDNHTESGVLYQIYE-MHPDADVYLHLGDSEfaYDDTELSLFNR------VKGNCDF-------YPEFENEAVAK 68
Cdd:cd00841    1 KIGVISDTHGNLEAIEKALElFEDGVDAVIHAGDFV--SPFVLNALLELkapliaVRGNNDGevdqllgRPILPEFLTLE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581832104  69 YNDVKAFYTHGHLYQVNRTRDLlaekGLELGCLFAFYGHTHVAKYEYINGVHVINPGSISQSRSSmEETYAEVIIDDQ 146
Cdd:cd00841   79 IGGLRILLTHGHLFGVLEALYL----AKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGG-RPTYAILDIEKL 151
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
26-152 8.31e-19

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 78.80  E-value: 8.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104  26 DADVYLHLGDSEFAYDDTE--LSLFNR-----VKGNCDFY-----PEFENEAVAKYNDVKAFYTHGHLYQV---NRTRDL 90
Cdd:COG0622   26 GVDLIVHLGDLVGYGPDPPevLDLLRElpivaVRGNHDGAvlrglRSLPETLRLELEGVRILLVHGSPNEYllpDTPAER 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581832104  91 LAEKGLELGCLFAFYGHTHVAKYEYINGVHVINPGSISQSRSSMEETYAEVIIDDQTLHGTI 152
Cdd:COG0622  106 LRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDGDPASYAILDIDDGEWSVEF 167
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 5-145 2.14e-17

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: 74.27  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104    5 IIVSDNHTESGVLYQIYEMHPDA-DVYLHLGD-SEFAYDDTELSL--FNRVKGNCD----FYPEFENEAVAKYNDVKAFY 76
Cdd:pfam12850   4 GIISDTHDNLALPEAALERLKGVvDLIIHAGDiVAPEVLEELLELapVLAVRGNNDaaaeFATDLPEEAVLELGGVKILL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581832104   77 THGHLYQVNRTRdlLAEKGLELGCLfAFYGHTHVAKYEYINGVHVINPGSISQSRSSMEETYAEVIIDD 145
Cdd:pfam12850  84 THGHGVKDALAR--LLRRAEEGVAV-VVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDIDD 149
PRK09453 PRK09453
phosphodiesterase; Provisional
 6-149 6.29e-16

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 71.05  E-value: 6.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104   6 IVSDNH-----TEsgVLYQIYEMHpDADVYLHLGDSEF---------AYDDTEL-SLFNR-------VKGNCDF------ 57
Cdd:PRK09453   5 FASDTHgslpaTE--KALELFAQS-GADWLVHLGDVLYhgprnplpeGYAPKKVaELLNAyadkiiaVRGNCDSevdqml 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104  58 --YPEFENEAVAKYNDVKAFYTHGHLYQvnrtrdllAEKGLEL-GCLFAFYGHTHVAKYEYINGVHVINPGSISQSRSSM 134
Cdd:PRK09453  82 lhFPIMAPYQQVLLEGKRLFLTHGHLYG--------PENLPALhDGDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGGY 153

                        170
                 ....*....|....*
gi 581832104 135 EETYAevIIDDQTLH 149
Cdd:PRK09453 154 PASYG--ILDDNVLS 166
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 6-145 2.78e-15

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: 68.94  E-value: 2.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104    6 IVSDNH---TESGVLYQIYEMHPDADVYLHLGDSEFAYDDTELSLFNR----VKGNCD-FYPEFENEAVAKYNDVKAFYT 77
Cdd:TIGR00040   5 VISDTHgplRATELPVELFNLESNVDLVIHAGDLTSPFVLKEFEDLAAkviaVRGNNDgERDELPEEEIFEAEGIDFGLV 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581832104   78 HGHLYQVNRTRDLLAEKGLELGCLFAFYGHTHVAKYEYINGVHVINPGSISQSRSSMEETYAEVIIDD 145
Cdd:TIGR00040  85 HGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSYAILDVDK 152
 
Name Accession Description Interval E-value
MPP_YfcE cd00841
Escherichia coli YfcE and related proteins, metallophosphatase domain; YfcE is a ...
 3-146 7.54e-24

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: 91.18  E-value: 7.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104   3 KWIIVSDNHTESGVLYQIYE-MHPDADVYLHLGDSEfaYDDTELSLFNR------VKGNCDF-------YPEFENEAVAK 68
Cdd:cd00841    1 KIGVISDTHGNLEAIEKALElFEDGVDAVIHAGDFV--SPFVLNALLELkapliaVRGNNDGevdqllgRPILPEFLTLE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581832104  69 YNDVKAFYTHGHLYQVNRTRDLlaekGLELGCLFAFYGHTHVAKYEYINGVHVINPGSISQSRSSmEETYAEVIIDDQ 146
Cdd:cd00841   79 IGGLRILLTHGHLFGVLEALYL----AKEGGADVVVFGHTHVPVIERVGGTLLLNPGSVSGPRGG-RPTYAILDIEKL 151
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
26-152 8.31e-19

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 78.80  E-value: 8.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104  26 DADVYLHLGDSEFAYDDTE--LSLFNR-----VKGNCDFY-----PEFENEAVAKYNDVKAFYTHGHLYQV---NRTRDL 90
Cdd:COG0622   26 GVDLIVHLGDLVGYGPDPPevLDLLRElpivaVRGNHDGAvlrglRSLPETLRLELEGVRILLVHGSPNEYllpDTPAER 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581832104  91 LAEKGLELGCLFAFYGHTHVAKYEYINGVHVINPGSISQSRSSMEETYAEVIIDDQTLHGTI 152
Cdd:COG0622  106 LRALAAEGDADVVVCGHTHIPFVRRVGGVLLVNPGSVGQPRDGDPASYAILDIDDGEWSVEF 167
Metallophos_2 pfam12850
Calcineurin-like phosphoesterase superfamily domain; Members of this family are part of the ...
 5-145 2.14e-17

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: 74.27  E-value: 2.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104    5 IIVSDNHTESGVLYQIYEMHPDA-DVYLHLGD-SEFAYDDTELSL--FNRVKGNCD----FYPEFENEAVAKYNDVKAFY 76
Cdd:pfam12850   4 GIISDTHDNLALPEAALERLKGVvDLIIHAGDiVAPEVLEELLELapVLAVRGNNDaaaeFATDLPEEAVLELGGVKILL 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 581832104   77 THGHLYQVNRTRdlLAEKGLELGCLfAFYGHTHVAKYEYINGVHVINPGSISQSRSSMEETYAEVIIDD 145
Cdd:pfam12850  84 THGHGVKDALAR--LLRRAEEGVAV-VVYGHTHVPGVERIGGVLFVNPGSVGGPRFGDPPTYALLDIDD 149
PRK09453 PRK09453
phosphodiesterase; Provisional
 6-149 6.29e-16

phosphodiesterase; Provisional


Pssm-ID: 181869 [Multi-domain]  Cd Length: 182  Bit Score: 71.05  E-value: 6.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104   6 IVSDNH-----TEsgVLYQIYEMHpDADVYLHLGDSEF---------AYDDTEL-SLFNR-------VKGNCDF------ 57
Cdd:PRK09453   5 FASDTHgslpaTE--KALELFAQS-GADWLVHLGDVLYhgprnplpeGYAPKKVaELLNAyadkiiaVRGNCDSevdqml 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104  58 --YPEFENEAVAKYNDVKAFYTHGHLYQvnrtrdllAEKGLEL-GCLFAFYGHTHVAKYEYINGVHVINPGSISQSRSSM 134
Cdd:PRK09453  82 lhFPIMAPYQQVLLEGKRLFLTHGHLYG--------PENLPALhDGDVLVYGHTHIPVAEKQGGIILFNPGSVSLPKGGY 153

                        170
                 ....*....|....*
gi 581832104 135 EETYAevIIDDQTLH 149
Cdd:PRK09453 154 PASYG--ILDDNVLS 166
yfcE TIGR00040
phosphoesterase, MJ0936 family; Members of this largely uncharacterized family share a motif ...
 6-145 2.78e-15

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: 68.94  E-value: 2.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104    6 IVSDNH---TESGVLYQIYEMHPDADVYLHLGDSEFAYDDTELSLFNR----VKGNCD-FYPEFENEAVAKYNDVKAFYT 77
Cdd:TIGR00040   5 VISDTHgplRATELPVELFNLESNVDLVIHAGDLTSPFVLKEFEDLAAkviaVRGNNDgERDELPEEEIFEAEGIDFGLV 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581832104   78 HGHLYQVNRTRDLLAEKGLELGCLFAFYGHTHVAKYEYINGVHVINPGSISQSRSSMEETYAEVIIDD 145
Cdd:TIGR00040  85 HGDLVYPRGDLLVLEYLAKELGVDVLIFGHTHIPVAEELRGILLINPGSLTGPRNGNTPSYAILDVDK 152
MPP_Vps29 cd07394
Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting ...
 76-128 4.58e-03

Homo sapiens Vps29 and related proteins, metallophosphatase domain; Vps29 (vacuolar sorting protein 29), also known as vacuolar membrane protein Pep11, is a subunit of the retromer complex which is responsible for the retrieval of mannose-6-phosphate receptors (MPRs) from the endosomes for retrograde transport back to the Golgi. Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer complex assembly as well as a phosphatase with specificity for the cytoplasmic tail of the MPR. The retromer includes the following 5 subunits: Vps35, Vps26, Vps29, and a dimer of the sorting nexins Vps5 (Snx1), and Vps17 (Snx2). Vps29 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: 163637 [Multi-domain]  Cd Length: 178  Bit Score: 36.03  E-value: 4.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 581832104  76 YTHGHLYQVNRTRDLLAEKGLELGCLFAFYGHTHVAKYEYINGVHVINPGSIS 128
Cdd:cd07394   83 LIHGHQVVPWGDPDSLAALQRQLDVDILISGHTHKFEAFEHEGKFFINPGSAT 135
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 5-125 4.89e-03

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: 35.32  E-value: 4.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581832104   5 IIVSDNHTESGVLYQIYEMH----PDADVYLHLGD-------SEFAYDDTELSLFNR-----VKGNCDFypefeneavak 68
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAAlakaEKPDLVICLGDlvdygpdPEEVELKALRLLLAGipvyvVPGNHDI----------- 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 581832104  69 yndvkaFYTHGHLYQVN--------RTRDLLAEKGLELGCLFAFYGHTHVAKYEYI--NGVHVINPG 125
Cdd:cd00838   70 ------LVTHGPPYDPLdegspgedPGSEALLELLDKYGPDLVLSGHTHVPGRREVdkGGTLVVNPG 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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