EzCatDB: M00020
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeM00020
RLCP classification3.103.90020.1134 : Transfer
CATH domainDomain 13.30.342.10 : DNA Polymerase; Chain A, domain 1
Domain 23.30.420.10 : Nucleotidyltransferase; domain 5
Domain 33.90.-.-Catalytic domain
Domain 41.-.-.-Catalytic domain
Domain 51.20.-.-
Domain 63.-.-.-
E.C.2.7.7.7

CATH domainRelated DB codes (homologues)
3.30.420.10 : Nucleotidyltransferase; domain 5M00206,T00252,M00019,M00055,M00135,M00146,M00166,M00173,M00175,M00186

Enzyme Name
UniProtKBKEGG

Q38087P04415
Protein nameDNA polymeraseDNA polymeraseDNA-directed DNA polymerase
DNA polymerase I
DNA polymerase II
DNA polymerase III
DNA polymerase alpha
DNA polymerase beta
DNA polymerase gamma
DNA nucleotidyltransferase (DNA-directed)
DNA nucleotidyltransferase (DNA-directed)
deoxyribonucleate nucleotidyltransferase
deoxynucleate polymerase
deoxyribonucleic acid duplicase
deoxyribonucleic acid polymerase
deoxyribonucleic duplicase
deoxyribonucleic polymerase
deoxyribonucleic polymerase I
DNA duplicase
DNA nucleotidyltransferase
DNA polymerase
DNA replicase
DNA-dependent DNA polymerase
duplicase
Klenow fragment
sequenase
Taq DNA polymerase
Taq Pol I
Tca DNA polymerase
SynonymsEC 2.7.7.7
Gp43
EC 2.7.7.7
Gp43
RefSeqNP_861746.1 (Protein)
NC_004928.1 (DNA/RNA sequence)
NP_049662.1 (Protein)
NC_000866.4 (DNA/RNA sequence)
PfamPF00136 (DNA_pol_B)
PF03104 (DNA_pol_B_exo1)
[Graphical view]
PF00136 (DNA_pol_B)
PF03104 (DNA_pol_B_exo1)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00230Purine metabolism
MAP00240Pyrimidine metabolism

UniProtKB:Accession NumberQ38087P04415
Entry nameDPOL_BPR69DPOL_BPT4
ActivityDeoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Subunit

Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC02148C00677C00039C00013C00039
CompoundDivalent metalDeoxynucleoside triphosphateDNA(n)PyrophosphateDNA(n+1)
Typedivalent metal (Ca2+, Mg2+)nucleotidenucleic acidsphosphate group/phosphate ionnucleic acids
ChEBI


29888

PubChem


21961011
1023

             
1clqA01UnboundUnboundUnboundUnboundUnbound
1ig9A01UnboundUnboundUnboundUnboundUnbound
1ih7A01UnboundUnboundUnboundUnboundUnbound
1q9xA01UnboundUnboundUnboundUnboundUnbound
1q9xB01UnboundUnboundUnboundUnboundUnbound
1q9xC01UnboundUnboundUnboundUnboundUnbound
1q9xD01UnboundUnboundUnboundUnboundUnbound
1q9yA01UnboundUnboundUnboundUnboundUnbound
1rv2A01UnboundUnboundUnboundUnboundUnbound
1rv2B01UnboundUnboundUnboundUnboundUnbound
1rv2C01UnboundUnboundUnboundUnboundUnbound
1rv2D01UnboundUnboundUnboundUnboundUnbound
1wafA01UnboundUnboundUnboundUnboundUnbound
1wafB01UnboundUnboundUnboundUnboundUnbound
1wajA01UnboundUnboundUnboundUnboundUnbound
1noyA01UnboundUnboundUnboundUnboundUnbound
1noyB01UnboundUnboundUnboundUnboundUnbound
1nozA01UnboundUnboundUnboundUnboundUnbound
1nozB01UnboundUnboundUnboundUnboundUnbound
1clqA02UnboundUnboundUnboundUnboundUnbound
1ig9A02UnboundUnboundUnboundUnboundUnbound
1ih7A02UnboundUnboundUnboundUnboundUnbound
1q9xA02UnboundUnboundUnboundUnboundUnbound
1q9xB02UnboundUnboundUnboundUnboundUnbound
1q9xC02UnboundUnboundUnboundUnboundUnbound
1q9xD02UnboundUnboundUnboundUnboundUnbound
1q9yA02UnboundUnboundUnboundUnboundUnbound
1rv2A02UnboundUnboundUnboundUnboundUnbound
1rv2B02UnboundUnboundUnboundUnboundUnbound
1rv2C02UnboundUnboundUnboundUnboundUnbound
1rv2D02UnboundUnboundUnboundUnboundUnbound
1wafA02UnboundUnboundUnboundUnboundUnbound
1wafB02UnboundUnboundUnboundUnboundUnbound
1wajA02UnboundUnboundUnboundUnboundUnbound
1noyA02UnboundUnboundUnboundUnboundUnbound
1noyB02UnboundUnboundUnboundUnboundUnbound
1nozA02UnboundUnboundUnboundUnboundUnbound
1nozB02UnboundUnboundUnboundUnboundUnbound
1clqA03Analogue:_CAUnboundUnboundUnboundUnbound
1ig9A03Analogue:2x_CABound:TTPAnalogue:G-C-G-G-A-C-T-G-C-T-T-A-C-DOC(chain P)UnboundUnbound
1ih7A03UnboundUnboundUnboundUnboundUnbound
1q9xA03Analogue:2x_CAUnboundAnalogue:G-C-G-G-A-C-T-G-C-T-T-A-C-DOC(chain I)UnboundUnbound
1q9xB03Analogue:2x_CAAnalogue:DGP 908Analogue:G-C-G-G-A-C-T-G-C-T-T-A-C-DOC(chain J)UnboundUnbound
1q9xC03Analogue:2x_CAAnalogue:DGP 908Analogue:G-C-G-G-A-C-T-G-C-T-T-A-C-DOC(chain K)UnboundUnbound
1q9xD03Analogue:2x_CAAnalogue:DGP 908Analogue:G-C-G-G-A-C-T-G-C-T-T-A-C-DOC(chain L)UnboundUnbound
1q9yA03Analogue:2x_CABound:DCPAnalogue:G-C-G-G-A-C-T-G-C-T-T-A-C-DOC(chain P)UnboundUnbound
1rv2A03UnboundUnboundUnboundUnboundBound:G-C-G-G-C-T-G-T-C-A-T-A-A-G-A(chain F)
1rv2B03UnboundUnboundUnboundUnboundUnbound
1rv2C03UnboundUnboundUnboundUnboundBound:G-C-G-G-C-T-G-T-C-A-T-A-A-G-A(chain J)
1rv2D03UnboundUnboundUnboundUnboundUnbound
1wafA03UnboundUnboundUnboundUnboundUnbound
1wafB03UnboundUnboundUnboundUnboundUnbound
1wajA03UnboundUnboundUnboundUnboundUnbound
1clqA04UnboundUnboundUnboundUnboundUnbound
1ig9A04UnboundUnboundUnboundUnboundUnbound
1ih7A04UnboundUnboundUnboundUnboundUnbound
1q9xA04UnboundUnboundUnboundUnboundUnbound
1q9xB04UnboundUnboundUnboundUnboundUnbound
1q9xC04UnboundUnboundUnboundUnboundUnbound
1q9xD04UnboundUnboundUnboundUnboundUnbound
1q9yA04UnboundUnboundUnboundUnboundUnbound
1rv2A04UnboundUnboundUnboundUnboundUnbound
1rv2B04UnboundUnboundUnboundUnboundUnbound
1rv2C04UnboundUnboundUnboundUnboundUnbound
1rv2D04UnboundUnboundUnboundUnboundUnbound
1wafA04UnboundUnboundUnboundUnboundUnbound
1wafB04UnboundUnboundUnboundUnboundUnbound
1wajA04UnboundUnboundUnboundUnboundUnbound
1clqA05UnboundUnboundUnboundUnboundUnbound
1ig9A05UnboundUnboundUnboundUnboundUnbound
1ih7A05UnboundUnboundUnboundUnboundUnbound
1q9xA05UnboundUnboundUnboundUnboundUnbound
1q9xB05UnboundUnboundUnboundUnboundUnbound
1q9xC05UnboundUnboundUnboundUnboundUnbound
1q9xD05UnboundUnboundUnboundUnboundUnbound
1q9yA05UnboundUnboundUnboundUnboundUnbound
1rv2A05UnboundUnboundUnboundUnboundUnbound
1rv2B05UnboundUnboundUnboundUnboundUnbound
1rv2C05UnboundUnboundUnboundUnboundUnbound
1rv2D05UnboundUnboundUnboundUnboundUnbound
1wafA05UnboundUnboundUnboundUnboundUnbound
1wafB05UnboundUnboundUnboundUnboundUnbound
1wajA05UnboundUnboundUnboundUnboundUnbound
1clqA06UnboundUnboundUnboundUnboundUnbound
1ig9A06UnboundUnboundUnboundUnboundUnbound
1ih7A06UnboundUnboundUnboundUnboundUnbound
1q9xA06UnboundUnboundUnboundUnboundUnbound
1q9xB06UnboundUnboundUnboundUnboundUnbound
1q9xC06UnboundUnboundUnboundUnboundUnbound
1q9xD06UnboundUnboundUnboundUnboundUnbound
1q9yA06UnboundUnboundUnboundUnboundUnbound
1rv2A06UnboundUnboundUnboundUnboundUnbound
1rv2B06UnboundUnboundUnboundUnboundUnbound
1rv2C06UnboundUnboundUnboundUnboundUnbound
1rv2D06UnboundUnboundUnboundUnboundUnbound
1wafA06UnboundUnboundUnboundUnboundUnbound
1wafB06UnboundUnboundUnboundUnboundUnbound
1wajA06UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [9]
pdbCatalytic residuesCofactor-binding residues
          
1clqA01 
 
1ig9A01 
 
1ih7A01 
 
1q9xA01 
 
1q9xB01 
 
1q9xC01 
 
1q9xD01 
 
1q9yA01 
 
1rv2A01 
 
1rv2B01 
 
1rv2C01 
 
1rv2D01 
 
1wafA01 
 
1wafB01 
 
1wajA01 
 
1noyA01 
 
1noyB01 
 
1nozA01 
 
1nozB01 
 
1clqA02 
 
1ig9A02 
 
1ih7A02 
 
1q9xA02 
 
1q9xB02 
 
1q9xC02 
 
1q9xD02 
 
1q9yA02 
 
1rv2A02 
 
1rv2B02 
 
1rv2C02 
 
1rv2D02 
 
1wafA02 
 
1wafB02 
 
1wajA02 
 
1noyA02 
 
1noyB02 
 
1nozA02 
 
1nozB02 
 
1clqA03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1ig9A03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1ih7A03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1q9xA03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1q9xB03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1q9xC03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1q9xD03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1q9yA03 
ASP 414;LEU 415;ASP 626;SER 627(metal binding)
1rv2A03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1rv2B03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1rv2C03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1rv2D03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1wafA03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1wafB03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1wajA03 
ASP 411;LEU 412;ASP 623;SER 624(metal binding)
1clqA04ARG 482;LYS 486;LYS 560;ASN 564
 
1ig9A04ARG 482;LYS 486;LYS 560;ASN 564
 
1ih7A04ARG 482;LYS 486;LYS 560;ASN 564
 
1q9xA04ARG 482;LYS 486;LYS 560;ASN 564
 
1q9xB04ARG 482;LYS 486;LYS 560;ASN 564
 
1q9xC04ARG 482;LYS 486;LYS 560;ASN 564
 
1q9xD04ARG 482;LYS 486;LYS 560;ASN 564
 
1q9yA04ARG 485;LYS 489;LYS 563;ASN 567
 
1rv2A04ARG 482;LYS 486;LYS 560;ASN 564
 
1rv2B04ARG 482;LYS 486;LYS 560;ASN 564
 
1rv2C04ARG 482;LYS 486;LYS 560;ASN 564
 
1rv2D04ARG 482;LYS 486;LYS 560;ASN 564
 
1wafA04ARG 482;LYS 486;LYS 560;ASN 564
 
1wafB04ARG 482;LYS 486;LYS 560;ASN 564
 
1wajA04ARG 482;LYS 486;LYS 560;ASN 564
 
1clqA05 
 
1ig9A05 
 
1ih7A05 
 
1q9xA05 
 
1q9xB05 
 
1q9xC05 
 
1q9xD05 
 
1q9yA05 
 
1rv2A05 
 
1rv2B05 
 
1rv2C05 
 
1rv2D05 
 
1wafA05 
 
1wafB05 
 
1wajA05 
 
1clqA06 
 
1ig9A06 
 
1ih7A06 
 
1q9xA06 
 
1q9xB06 
 
1q9xC06 
 
1q9xD06 
 
1q9yA06 
 
1rv2A06 
 
1rv2B06 
 
1rv2C06 
 
1rv2D06 
 
1wafA06 
 
1wafB06 
 
1wajA06 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]Fig.3, p.1922
[9]Fig.4, p.61
[11]p.8100
[20]p.661-665

references
[1]
PubMed ID1349852
JournalCell
Year1992
Volume69
Pages425-37
AuthorsKong XP, Onrust R, O'Donnell M, Kuriyan J
TitleThree-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp.
[2]
PubMed ID1314195
JournalFEBS Lett
Year1992
Volume300
Pages141-4
AuthorsStrick R, Knopf CW
TitleImproved band shift assay for the simultaneous analysis of protein-DNA interactions and enzymatic functions of DNA polymerases.
[3]
PubMed ID7903401
JournalJ Mol Biol
Year1993
Volume234
Pages915-25
AuthorsKuriyan J, O'Donnell M
TitleSliding clamps of DNA polymerases.
[4]
PubMed ID8594347
JournalMethods Enzymol
Year1995
Volume262
Pages189-202
AuthorsEckstein F, Thomson JB
TitlePhosphate analogs for study of DNA polymerases.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-388.
Medline ID96292335
PubMed ID8679562
JournalBiochemistry
Year1996
Volume35
Pages8110-9
AuthorsWang J, Yu P, Lin TC, Konigsberg WH, Steitz TA
TitleCrystal structures of an NH2-terminal fragment of T4 DNA polymerase and its complexes with single-stranded DNA and with divalent metal ions.
Related PDB1noy,1noz
Related UniProtKBP04415
[6]
PubMed ID9265627
JournalBiochemistry
Year1997
Volume36
Pages10474-81
AuthorsGoodrich LD, Lin TC, Spicer EK, Jones C, Konigsberg WH
TitleResidues at the carboxy terminus of T4 DNA polymerase are important determinants for interaction with the polymerase accessory proteins.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID97358535
PubMed ID9215631
JournalCell
Year1997
Volume89
Pages1087-99
AuthorsWang J, Sattar AK, Wang CC, Karam JD, Konigsberg WH, Steitz TA
TitleCrystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69.
Related PDB1waf,1waj
Related UniProtKBQ38087
[8]
PubMed ID9665721
JournalBiochemistry
Year1998
Volume37
Pages10156-63
AuthorsOtto MR, Bloom LB, Goodman MF, Beechem JM
TitleStopped-flow fluorescence study of precatalytic primer strand base-unstacking transitions in the exonuclease cleft of bacteriophage T4 DNA polymerase.
[9]
PubMed ID9519297
JournalCurr Opin Struct Biol
Year1998
Volume8
Pages54-63
AuthorsBrautigam CA, Steitz TA
TitleStructural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes.
[10]
PubMed ID10387009
JournalBiochemistry
Year1999
Volume38
Pages7696-709
AuthorsAlley SC, Shier VK, Abel-Santos E, Sexton DJ, Soumillion P, Benkovic SJ
TitleSliding clamp of the bacteriophage T4 polymerase has open and closed subunit interfaces in solution.
[11]
PubMed ID10387055
JournalBiochemistry
Year1999
Volume38
Pages8094-101
AuthorsYang G, Lin T, Karam J, Konigsberg WH
TitleSteady-state kinetic characterization of RB69 DNA polymerase mutants that affect dNTP incorporation.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH GP45.
Medline ID20004392
PubMed ID10535734
JournalCell
Year1999
Volume99
Pages155-66
AuthorsShamoo Y, Steitz TA
TitleBuilding a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex.
Related PDB1clq,1b8h
Related UniProtKBQ38087
[13]
PubMed ID10616725
JournalNucleosides Nucleotides
Year1999
Volume18
Pages2193-9
AuthorsStattel JM, Wright GE
TitleSensitivity of bacteriophage RB69 DNA polymerase to N2-(p-n-butylphenyl)-2'-deoxyguanosine nucleotides.
[14]
PubMed ID10097083
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages3600-5
AuthorsHopfner KP, Eichinger A, Engh RA, Laue F, Ankenbauer W, Huber R, Angerer B
TitleCrystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius.
[15]
PubMed ID10545321
JournalStructure Fold Des
Year1999
Volume7
Pages1189-99
AuthorsZhao Y, Jeruzalmi D, Moarefi I, Leighton L, Lasken R, Kuriyan J
TitleCrystal structure of an archaebacterial DNA polymerase.
[16]
PubMed ID10860752
JournalJ Mol Biol
Year2000
Volume299
Pages447-62
AuthorsRodriguez AC, Park HW, Mao C, Beese LS
TitleCrystal structure of a pol alpha family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. 9 degrees N-7.
[17]
PubMed ID11401565
JournalBiochemistry
Year2001
Volume40
Pages7180-91
AuthorsBerdis AJ
TitleDynamics of translesion DNA synthesis catalyzed by the bacteriophage T4 exonuclease-deficient DNA polymerase.
[18]
PubMed ID11504721
JournalJ Biol Chem
Year2001
Volume276
Pages39340-9
AuthorsAlley SC, Trakselis MA, Mayer MU, Ishmael FT, Jones AD, Benkovic SJ
TitleBuilding a replisome solution structure by elucidation of protein-protein interactions in the bacteriophage T4 DNA polymerase holoenzyme.
[19]
PubMed ID11178906
JournalJ Mol Biol
Year2001
Volume306
Pages469-77
AuthorsHashimoto H, Nishioka M, Fujiwara S, Takagi M, Imanaka T, Inoue T, Kai Y
TitleCrystal structure of DNA polymerase from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1.
[20]
PubMed ID11389835
JournalCell
Year2001
Volume105
Pages657-67
AuthorsFranklin MC, Wang J, Steitz TA
TitleStructure of the replicating complex of a pol alpha family DNA polymerase.
Related PDB1ig9,1ih7
[21]
PubMed ID12162740
JournalBiochemistry
Year2002
Volume41
Pages10256-61
AuthorsYang G, Franklin M, Li J, Lin TC, Konigsberg W
TitleA conserved Tyr residue is required for sugar selectivity in a Pol alpha DNA polymerase.
[22]
PubMed ID12087102
JournalJ Biol Chem
Year2002
Volume277
Pages33041-8
AuthorsPetrov VM, Ng SS, Karam JD
TitleProtein determinants of RNA binding by DNA polymerase of the T4-related bacteriophage RB69.
[23]
PubMed ID12415300
JournalNat Rev Mol Cell Biol
Year2002
Volume3
Pages826-35
AuthorsDavey MJ, Jeruzalmi D, Kuriyan J, O'Donnell M
TitleMotors and switches: AAA+ machines within the replisome.
[24]
PubMed ID15057283
JournalEMBO J
Year2004
Volume23
Pages1483-93
AuthorsHogg M, Wallace SS, Doublie S
TitleCrystallographic snapshots of a replicative DNA polymerase encountering an abasic site.
Related PDB1rv2
[25]
PubMed ID15057282
JournalEMBO J
Year2004
Volume23
Pages1494-505
AuthorsFreisinger E, Grollman AP, Miller H, Kisker C
TitleLesion (in)tolerance reveals insights into DNA replication fidelity.
Related PDB1q9x,1q9y

comments
This enzyme belongs to the DNA polymerase type-B family.
In the CATH definition, this enzyme has got six domains. The second domain seems to have exonuclease activity, although it is not annotated in this entry. The third and fourth domains have polymerase activity.
On the third domain, two divalent metal ions such as magnesium ions and manganese ions are bound to two acidic residues. One of the metal ion, A, is bound to alpha-phosphate oxygen of deoxynucletide triphosphate (dNTP), and 3'-OH of the primer DNA. The other metal ion, B, is bound to oxgens from all three phosphate of the dNTP (see [9]).
According to the literature [9] & [11], the catalytic reaction of polymerase domains proceeds as follows:
(1) The metal ion A activates 3'-OH of DNA by lowering its pKa.
(2) The activated 3'-O atom makes a nucleophilic attack on the alpha-phosphate group of dNTP, forming a pentacoordinated transition-state.
(3) The negative charges on the transferred group (alpha-phoshate) and the leaving group (beta-phosphate and gamma-phosphate) are stabilized by the metal ions and stabilizers on the fourth domain (Arg482, Lys486, Lys560 & Asn564). According to the literature [11], Lys560 stabilizes the transferred alpha-phosphate, which is also stabilzed by both A and B metal ions. Asn564 stabilizes beta-phosphate, along with the metal ion B, Arg482 and Lys486 stabilize gamma-phosphate together with the metal ion B (see [11]). (Arg482 and Lys486 are more important than Lys560 and Asn564, according to the literature [11].)

createdupdated
2004-03-032009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.