DPOL_BPT7
ID DPOL_BPT7 Reviewed; 704 AA.
AC P00581;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000255|HAMAP-Rule:MF_04101};
DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_04101, ECO:0000269|PubMed:24591606};
DE EC=3.1.11.- {ECO:0000255|HAMAP-Rule:MF_04101, ECO:0000269|PubMed:15292168, ECO:0000269|PubMed:2703498};
DE AltName: Full=Gene product 5;
DE Short=Gp5;
GN OrderedLocusNames=5;
OS Escherichia phage T7 (Bacteriophage T7).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX NCBI_TaxID=10760;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA Dunn J.J., Studier F.W.;
RT "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT T7 genetic elements.";
RL J. Mol. Biol. 166:477-535(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6708104; DOI=10.1016/0022-2836(84)90194-3;
RA Moffatt B.A., Dunn J.J., Studier F.W.;
RT "Nucleotide sequence of the gene for bacteriophage T7 RNA polymerase.";
RL J. Mol. Biol. 173:265-269(1984).
RN [3]
RP FUNCTION, MUTAGENESIS OF HIS-123, AND CATALYTIC ACTIVITY.
RX PubMed=2703498; DOI=10.1016/s0021-9258(18)83369-5;
RA Tabor S., Richardson C.C.;
RT "Selective inactivation of the exonuclease activity of bacteriophage T7 DNA
RT polymerase by in vitro mutagenesis.";
RL J. Biol. Chem. 264:6447-6458(1989).
RN [4]
RP FUNCTION, AND INTERACTION WITH PROTEIN GP4.
RX PubMed=9218486; DOI=10.1074/jbc.272.29.18425;
RA Notarnicola S.M., Mulcahy H.L., Lee J., Richardson C.C.;
RT "The acidic carboxyl terminus of the bacteriophage T7 gene 4
RT helicase/primase interacts with T7 DNA polymerase.";
RL J. Biol. Chem. 272:18425-18433(1997).
RN [5]
RP COFACTOR.
RX PubMed=9914251; DOI=10.1016/s0959-440x(98)80089-4;
RA Doublie S., Ellenberger T.;
RT "The mechanism of action of T7 DNA polymerase.";
RL Curr. Opin. Struct. Biol. 8:704-712(1998).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15292168; DOI=10.1074/jbc.m406103200;
RA Kumar J.K., Chiu E.T., Tabor S., Richardson C.C.;
RT "A unique region in bacteriophage t7 DNA polymerase important for
RT exonucleolytic hydrolysis of DNA.";
RL J. Biol. Chem. 279:42018-42025(2004).
RN [7]
RP INTERACTION WITH THE SSDNA-BINDING PROTEIN; DNA PRIMASE/HELICASE AND HOST
RP TRXA, AND IDENTIFICATION IN THE REPLICASE COMPLEX.
RX PubMed=15795374; DOI=10.1073/pnas.0501637102;
RA Hamdan S.M., Marintcheva B., Cook T., Lee S.J., Tabor S., Richardson C.C.;
RT "A unique loop in T7 DNA polymerase mediates the binding of helicase-
RT primase, DNA binding protein, and processivity factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5096-5101(2005).
RN [8]
RP REVIEW ON FUNCTION.
RX PubMed=21907611; DOI=10.1016/j.cbpa.2011.07.024;
RA Lee S.J., Richardson C.C.;
RT "Choreography of bacteriophage T7 DNA replication.";
RL Curr. Opin. Chem. Biol. 15:580-586(2011).
RN [9]
RP FUNCTION.
RX PubMed=21606333; DOI=10.1073/pnas.1106678108;
RA Zhang H., Lee S.J., Zhu B., Tran N.Q., Tabor S., Richardson C.C.;
RT "Helicase-DNA polymerase interaction is critical to initiate leading-strand
RT DNA synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9372-9377(2011).
RN [10]
RP CATALYTIC ACTIVITY.
RX PubMed=24591606; DOI=10.1073/pnas.1402010111;
RA Geertsema H.J., Kulczyk A.W., Richardson C.C., van Oijen A.M.;
RT "Single-molecule studies of polymerase dynamics and stoichiometry at the
RT bacteriophage T7 replication machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4073-4078(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MANGANESE AND ZINC,
RP AND COFACTOR.
RX PubMed=9440688; DOI=10.1038/34593;
RA Doublie S., Tabor S., Long A.M., Richardson C.C., Ellenberger T.;
RT "Crystal structure of a bacteriophage T7 DNA replication complex at 2.2-A
RT resolution.";
RL Nature 391:251-258(1998).
CC -!- FUNCTION: Replicates viral genomic DNA. This polymerase possesses two
CC enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic
CC activity that degrades single-stranded DNA in the 3'-5' direction (By
CC similarity). Non-processive DNA polymerase that achieves processivity
CC by binding to host thioredoxin (TrxA). This interaction increases the
CC rate of dNTP incorporation to yield a processivity of approximately 800
CC nucleotides (nt) per binding event. Interacts with DNA helicase gp4 to
CC coordinate nucleotide polymerization with unwinding of the DNA. The
CC leading strand is synthesized continuously while synthesis of the
CC lagging strand requires the synthesis of oligoribonucleotides by the
CC primase domain of gp4. {ECO:0000255|HAMAP-Rule:MF_04101,
CC ECO:0000269|PubMed:15292168, ECO:0000269|PubMed:21606333,
CC ECO:0000269|PubMed:2703498, ECO:0000269|PubMed:9218486}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_04101, ECO:0000269|PubMed:24591606};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04101,
CC ECO:0000305|PubMed:9440688};
CC -!- SUBUNIT: Composed of two subunits. One is encoded by the phage and the
CC other is encoded by the host thioredoxin. Interacts with DNA
CC primase/helicase; this interaction is essential for the coordination of
CC DNA unwinding and nucleotide polymerization on duplex DNA. Interacts
CC with the ssDNA-binding protein. Part of the replicase complex that
CC includes the DNA polymerase, thioredoxin, the primase/helicase and the
CC single-stranded DNA binding protein. {ECO:0000269|PubMed:15795374,
CC ECO:0000269|PubMed:9218486}.
CC -!- INTERACTION:
CC P00581; P03692: 4; NbExp=2; IntAct=EBI-8664634, EBI-8664802;
CC P00581; P0AA25: trxA; Xeno; NbExp=2; IntAct=EBI-8664634, EBI-368542;
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000255|HAMAP-Rule:MF_04101}.
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DR EMBL; V01146; CAA24412.1; -; Genomic_DNA.
DR PIR; A00716; DJBPT7.
DR RefSeq; NP_041982.1; NC_001604.1.
DR PDB; 1SKR; X-ray; 2.40 A; A=1-704.
DR PDB; 1SKS; X-ray; 2.30 A; A=1-704.
DR PDB; 1SKW; X-ray; 2.30 A; A=1-704.
DR PDB; 1SL0; X-ray; 3.20 A; A/C=1-704.
DR PDB; 1SL1; X-ray; 2.20 A; A=1-704.
DR PDB; 1SL2; X-ray; 2.30 A; A=1-704.
DR PDB; 1T7P; X-ray; 2.20 A; A=1-704.
DR PDB; 1T8E; X-ray; 2.54 A; A=1-704.
DR PDB; 1TK0; X-ray; 2.30 A; A=1-704.
DR PDB; 1TK5; X-ray; 2.20 A; A=1-704.
DR PDB; 1TK8; X-ray; 2.50 A; A=1-704.
DR PDB; 1TKD; X-ray; 2.49 A; A=1-704.
DR PDB; 1X9M; X-ray; 2.10 A; A=1-704.
DR PDB; 1X9S; X-ray; 2.70 A; A=1-704.
DR PDB; 1X9W; X-ray; 2.30 A; A=1-704.
DR PDB; 1ZYQ; X-ray; 2.70 A; A=1-698.
DR PDB; 2AJQ; X-ray; 2.60 A; A/F=1-704.
DR PDB; 5IKN; X-ray; 4.80 A; A/B/C=1-704.
DR PDB; 6N7W; EM; 4.50 A; H=1-704.
DR PDB; 6N9U; EM; 3.70 A; H=1-704.
DR PDB; 6N9V; EM; 4.00 A; H=1-704.
DR PDB; 6N9W; EM; 4.00 A; H=1-704.
DR PDB; 6N9X; EM; 4.10 A; H=1-704.
DR PDB; 6P7E; X-ray; 3.00 A; A/B/C/D=1-704.
DR PDBsum; 1SKR; -.
DR PDBsum; 1SKS; -.
DR PDBsum; 1SKW; -.
DR PDBsum; 1SL0; -.
DR PDBsum; 1SL1; -.
DR PDBsum; 1SL2; -.
DR PDBsum; 1T7P; -.
DR PDBsum; 1T8E; -.
DR PDBsum; 1TK0; -.
DR PDBsum; 1TK5; -.
DR PDBsum; 1TK8; -.
DR PDBsum; 1TKD; -.
DR PDBsum; 1X9M; -.
DR PDBsum; 1X9S; -.
DR PDBsum; 1X9W; -.
DR PDBsum; 1ZYQ; -.
DR PDBsum; 2AJQ; -.
DR PDBsum; 5IKN; -.
DR PDBsum; 6N7W; -.
DR PDBsum; 6N9U; -.
DR PDBsum; 6N9V; -.
DR PDBsum; 6N9W; -.
DR PDBsum; 6N9X; -.
DR PDBsum; 6P7E; -.
DR SMR; P00581; -.
DR DIP; DIP-41665N; -.
DR IntAct; P00581; 5.
DR MINT; P00581; -.
DR PRIDE; P00581; -.
DR GeneID; 1261044; -.
DR KEGG; vg:1261044; -.
DR EvolutionaryTrace; P00581; -.
DR Proteomes; UP000000840; Genome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IMP:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:FlyBase.
DR GO; GO:0004529; F:exodeoxyribonuclease activity; IMP:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0090592; P:DNA synthesis involved in DNA replication; IMP:CACAO.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:FlyBase.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_04101; DPOL_T7; 1.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR034699; DPOL_T7.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; PTHR10133; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Exonuclease; Host-virus interaction; Hydrolase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW Reference proteome; Transferase; Viral DNA replication.
FT CHAIN 1..704
FT /note="DNA-directed DNA polymerase"
FT /id="PRO_0000101269"
FT REGION 1..187
FT /note="3'-5'exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000269|PubMed:9440688"
FT REGION 202..704
FT /note="Polymerase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000305|PubMed:9440688"
FT REGION 262..338
FT /note="Binding to host TrxA"
FT /evidence="ECO:0000269|PubMed:15795374,
FT ECO:0000303|PubMed:15292168"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000305|PubMed:9440688"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000305|PubMed:9440688"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000305|PubMed:9440688"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000305|PubMed:9440688"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000269|PubMed:9440688, ECO:0000305|PubMed:9914251"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000269|PubMed:9440688, ECO:0000305|PubMed:9914251"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000269|PubMed:9440688, ECO:0000305|PubMed:9914251"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000305|PubMed:9914251"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000305|PubMed:9914251"
FT BINDING 522
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000305|PubMed:9914251"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000305|PubMed:9914251"
FT BINDING 654
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000269|PubMed:9440688, ECO:0000305|PubMed:9914251"
FT BINDING 654
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101,
FT ECO:0000269|PubMed:9440688, ECO:0000305|PubMed:9914251"
FT MUTAGEN 123
FT /note="H->S: 83% loss of exonuclease activity."
FT /evidence="ECO:0000269|PubMed:2703498"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:1X9M"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1X9M"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:1X9M"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1X9M"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2AJQ"
FT HELIX 127..149
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 165..186
FT /evidence="ECO:0007829|PDB:1X9M"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2AJQ"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 212..230
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 236..260
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:1X9M"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1SL2"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:1TK5"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1TK5"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:1X9M"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:1T7P"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 377..399
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:1SKS"
FT HELIX 448..453
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:1X9M"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 470..476
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 479..492
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 495..502
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 505..512
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 518..529
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 534..538
FT /evidence="ECO:0007829|PDB:1X9M"
FT TURN 539..542
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 545..557
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 560..571
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:1TK0"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:1T8E"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:1TK0"
FT STRAND 591..594
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 609..635
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 644..652
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 655..662
FT /evidence="ECO:0007829|PDB:1X9M"
FT HELIX 663..683
FT /evidence="ECO:0007829|PDB:1X9M"
FT STRAND 692..699
FT /evidence="ECO:0007829|PDB:1X9M"
FT TURN 700..703
FT /evidence="ECO:0007829|PDB:1X9M"
SQ SEQUENCE 704 AA; 79692 MW; 17089CE2AD9FB596 CRC64;
MIVSDIEANA LLESVTKFHC GVIYDYSTAE YVSYRPSDFG AYLDALEAEV ARGGLIVFHN
GHKYDVPALT KLAKLQLNRE FHLPRENCID TLVLSRLIHS NLKDTDMGLL RSGKLPGKRF
GSHALEAWGY RLGEMKGEYK DDFKRMLEEQ GEEYVDGMEW WNFNEEMMDY NVQDVVVTKA
LLEKLLSDKH YFPPEIDFTD VGYTTFWSES LEAVDIEHRA AWLLAKQERN GFPFDTKAIE
ELYVELAARR SELLRKLTET FGSWYQPKGG TEMFCHPRTG KPLPKYPRIK TPKVGGIFKK
PKNKAQREGR EPCELDTREY VAGAPYTPVE HVVFNPSSRD HIQKKLQEAG WVPTKYTDKG
APVVDDEVLE GVRVDDPEKQ AAIDLIKEYL MIQKRIGQSA EGDKAWLRYV AEDGKIHGSV
NPNGAVTGRA THAFPNLAQI PGVRSPYGEQ CRAAFGAEHH LDGITGKPWV QAGIDASGLE
LRCLAHFMAR FDNGEYAHEI LNGDIHTKNQ IAAELPTRDN AKTFIYGFLY GAGDEKIGQI
VGAGKERGKE LKKKFLENTP AIAALRESIQ QTLVESSQWV AGEQQVKWKR RWIKGLDGRK
VHVRSPHAAL NTLLQSAGAL ICKLWIIKTE EMLVEKGLKH GWDGDFAYMA WVHDEIQVGC
RTEEIAQVVI ETAQEAMRWV GDHWNFRCLL DTEGKMGPNW AICH
