DPOL_BPT4
ID DPOL_BPT4 Reviewed; 898 AA.
AC P04415;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000255|HAMAP-Rule:MF_04100};
DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:1332748};
DE EC=3.1.11.- {ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:10455197, ECO:0000269|PubMed:1332748, ECO:0000269|PubMed:15037066, ECO:0000269|PubMed:8262948};
DE AltName: Full=Gene product 43;
DE Short=Gp43;
GN Name=43;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3286635; DOI=10.1016/s0021-9258(18)68523-0;
RA Spicer E.K., Rush J., Fung C., Reha-Krantz L.J., Karam J.D.,
RA Konigsberg W.H.;
RT "Primary structure of T4 DNA polymerase. Evolutionary relatedness to
RT eucaryotic and other procaryotic DNA polymerases.";
RL J. Biol. Chem. 263:7478-7486(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3054876; DOI=10.1073/pnas.85.21.7942;
RA Andrake M., Guild N., Hsu T., Gold L., Tuerk C., Karam J.;
RT "DNA polymerase of bacteriophage T4 is an autogenous translational
RT repressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7942-7946(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-898.
RX PubMed=3350013; DOI=10.1111/j.1432-1033.1988.tb13925.x;
RA Lamm N., Wang Y., Mathews C.K., Rueger W.;
RT "Deoxycytidylate hydroxymethylase gene of bacteriophage T4. Nucleotide
RT sequence determination and over-expression of the gene.";
RL Eur. J. Biochem. 172:553-563(1988).
RN [5]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=1332748; DOI=10.1021/bi00160a007;
RA Capson T.L., Peliska J.A., Kaboord B.F., Frey M.W., Lively C., Dahlberg M.,
RA Benkovic S.J.;
RT "Kinetic characterization of the polymerase and exonuclease activities of
RT the gene 43 protein of bacteriophage T4.";
RL Biochemistry 31:10984-10994(1992).
RN [6]
RP INTERACTION WITH THE POLYMERASE CLAMP.
RX PubMed=8475061; DOI=10.1073/pnas.90.8.3211;
RA Reddy M.K., Weitzel S.E., von Hippel P.H.;
RT "Assembly of a functional replication complex without ATP hydrolysis: a
RT direct interaction of bacteriophage T4 gp45 with T4 DNA polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3211-3215(1993).
RN [7]
RP MUTAGENESIS OF ASP-112; GLU-114; ASP-219 AND ASP-324, AND CATALYTIC
RP ACTIVITY.
RX PubMed=8262948; DOI=10.1016/s0021-9258(19)74223-9;
RA Reha-Krantz L.J., Nonay R.L.;
RT "Genetic and biochemical studies of bacteriophage T4 DNA polymerase
RT 3'-->5'-exonuclease activity.";
RL J. Biol. Chem. 268:27100-27108(1993).
RN [8]
RP DOMAIN.
RX PubMed=7592876; DOI=10.1074/jbc.270.44.26558;
RA Wang C.C., Yeh L.-S., Karam J.D.;
RT "Modular organization of T4 DNA polymerase. Evidence from phylogenetics.";
RL J. Biol. Chem. 270:26558-26564(1995).
RN [9]
RP INTERACTION WITH THE POLYMERASE CLAMP.
RX PubMed=8917503; DOI=10.1073/pnas.93.23.12822;
RA Berdis A.J., Soumillion P., Benkovic S.J.;
RT "The carboxyl terminus of the bacteriophage T4 DNA polymerase is required
RT for holoenzyme complex formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12822-12827(1996).
RN [10]
RP COFACTOR.
RX PubMed=9665720; DOI=10.1021/bi980074b;
RA Beechem J.M., Otto M.R., Bloom L.B., Eritja R., Reha-Krantz L.J.,
RA Goodman M.F.;
RT "Exonuclease-polymerase active site partitioning of primer-template DNA
RT strands and equilibrium Mg2+ binding properties of bacteriophage T4 DNA
RT polymerase.";
RL Biochemistry 37:10144-10155(1998).
RN [11]
RP INTERACTION WITH THE DNA HELICASE ASSEMBLY PROTEIN.
RX PubMed=15909989; DOI=10.1021/bi047296w;
RA Xi J., Zhang Z., Zhuang Z., Yang J., Spiering M.M., Hammes G.G.,
RA Benkovic S.J.;
RT "Interaction between the T4 helicase loading protein (gp59) and the DNA
RT polymerase (gp43): unlocking of the gp59-gp43-DNA complex to initiate
RT assembly of a fully functional replisome.";
RL Biochemistry 44:7747-7756(2005).
RN [12]
RP IDENTIFICATION IN THE REPLICASE COMPLEX.
RX PubMed=16800624; DOI=10.1021/bi0603322;
RA Smiley R.D., Zhuang Z., Benkovic S.J., Hammes G.G.;
RT "Single-molecule investigation of the T4 bacteriophage DNA polymerase
RT holoenzyme: multiple pathways of holoenzyme formation.";
RL Biochemistry 45:7990-7997(2006).
RN [13]
RP CATALYTIC ACTIVITY.
RX PubMed=10455197; DOI=10.1074/jbc.274.35.25151;
RA Elisseeva E., Mandal S.S., Reha-Krantz L.J.;
RT "Mutational and pH studies of the 3' --> 5' exonuclease activity of
RT bacteriophage T4 DNA polymerase.";
RL J. Biol. Chem. 274:25151-25158(1999).
RN [14]
RP FUNCTION, MUTAGENESIS OF ASP-219, AND CATALYTIC ACTIVITY.
RX PubMed=15037066; DOI=10.1016/j.jmb.2004.01.005;
RA Tanguy Le Gac N., Delagoutte E., Germain M., Villani G.;
RT "Inactivation of the 3'-5' exonuclease of the replicative T4 DNA polymerase
RT allows translesion DNA synthesis at an abasic site.";
RL J. Mol. Biol. 336:1023-1034(2004).
RN [15]
RP REVIEW.
RX PubMed=21129204; DOI=10.1186/1743-422x-7-359;
RA Mueser T.C., Hinerman J.M., Devos J.M., Boyer R.A., Williams K.J.;
RT "Structural analysis of bacteriophage T4 DNA replication: a review in the
RT Virology Journal series on bacteriophage T4 and its relatives.";
RL Virol. J. 7:359-359(2010).
RN [16]
RP DOMAIN.
RX PubMed=25753811; DOI=10.1016/j.dnarep.2015.02.014;
RA Darmawan H., Harrison M., Reha-Krantz L.J.;
RT "DNA polymerase 3'->5' exonuclease activity: Different roles of the beta
RT hairpin structure in family-B DNA polymerases.";
RL DNA Repair 29:36-46(2015).
RN [17]
RP REVIEW, AND SUBUNIT.
RX PubMed=26102578; DOI=10.3390/v7062766;
RA Noble E., Spiering M.M., Benkovic S.J.;
RT "Coordinated DNA replication by the bacteriophage T4 replisome.";
RL Viruses 7:3186-3200(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-388.
RX PubMed=8679562; DOI=10.1021/bi960178r;
RA Wang J., Yu P., Lin T.C., Konigsberg W.H., Steitz T.A.;
RT "Crystal structures of an NH2-terminal fragment of T4 DNA polymerase and
RT its complexes with single-stranded DNA and with divalent metal ions.";
RL Biochemistry 35:8110-8119(1996).
CC -!- FUNCTION: Replicates the viral genomic DNA. This polymerase possesses
CC two enzymatic activities: DNA synthesis (polymerase) and an
CC exonucleolytic activity that degrades single-stranded DNA in the 3'- to
CC 5'-direction for proofreading purpose. {ECO:0000255|HAMAP-
CC Rule:MF_04100, ECO:0000269|PubMed:1332748,
CC ECO:0000269|PubMed:15037066}.
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_04100, ECO:0000269|PubMed:1332748};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04100,
CC ECO:0000269|PubMed:9665720};
CC -!- SUBUNIT: Interacts with the polymerase clamp; this interaction
CC constitutes the polymerase holoenzyme (PubMed:8475061, PubMed:8917503).
CC Interacts with the helicase assembly factor (PubMed:15909989). Part of
CC the replicase complex that includes the DNA polymerase, the polymerase
CC clamp, the clamp loader complex, the single-stranded DNA binding
CC protein, the primase, the helicase and the helicase assembly factor
CC (PubMed:16800624). {ECO:0000269|PubMed:15909989,
CC ECO:0000269|PubMed:16800624, ECO:0000269|PubMed:8475061,
CC ECO:0000269|PubMed:8917503}.
CC -!- DOMAIN: The N-terminus contains the 3'-5' exonuclease activity
CC (PubMed:7592876). The C-terminus contains the polymerase activity and
CC is involved in binding to the polymerase clamp protein
CC (PubMed:7592876). A beta hairpin structure is necessary for the
CC proofreading function of the polymerase (PubMed:25753811).
CC {ECO:0000255|HAMAP-Rule:MF_04100, ECO:0000269|PubMed:25753811,
CC ECO:0000269|PubMed:7592876}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000255|HAMAP-Rule:MF_04100}.
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DR EMBL; M10160; AAC05397.1; -; Genomic_DNA.
DR EMBL; X00769; CAA25344.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42468.1; -; Genomic_DNA.
DR EMBL; M37159; AAA21706.1; -; Genomic_DNA.
DR PIR; JS0791; DJBPT4.
DR RefSeq; NP_049662.1; NC_000866.4.
DR PDB; 1NOY; X-ray; 2.20 A; A/B=1-388.
DR PDB; 1NOZ; X-ray; 2.20 A; A/B=1-388.
DR PDBsum; 1NOY; -.
DR PDBsum; 1NOZ; -.
DR SMR; P04415; -.
DR BindingDB; P04415; -.
DR ChEMBL; CHEMBL5946; -.
DR GeneID; 1258685; -.
DR KEGG; vg:1258685; -.
DR BRENDA; 2.7.7.7; 732.
DR SABIO-RK; P04415; -.
DR EvolutionaryTrace; P04415; -.
DR PRO; PR:P04415; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR HAMAP; MF_04100; DPOL_T4; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR034749; DPOL_T4.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Exonuclease; Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Nuclease; Nucleotidyltransferase; Reference proteome; Transferase;
KW Viral DNA replication.
FT CHAIN 1..898
FT /note="DNA-directed DNA polymerase"
FT /id="PRO_0000046546"
FT REGION 101..337
FT /note="3'-5'exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04100,
FT ECO:0000269|PubMed:7592876"
FT REGION 245..261
FT /note="Beta hairpin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04100,
FT ECO:0000269|PubMed:25753811"
FT REGION 377..898
FT /note="Polymerase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04100,
FT ECO:0000269|PubMed:7592876"
FT REGION 702..705
FT /note="Binding of DNA in B-conformation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04100"
FT REGION 893..898
FT /note="Interaction with the polymerase clamp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04100,
FT ECO:0000269|PubMed:8917503"
FT BINDING 112
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_04100,
FT ECO:0000269|PubMed:8679562"
FT BINDING 114
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_04100,
FT ECO:0000269|PubMed:8679562"
FT BINDING 219
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_04100,
FT ECO:0000269|PubMed:8679562"
FT BINDING 324
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_04100,
FT ECO:0000269|PubMed:8679562"
FT BINDING 324
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_04100,
FT ECO:0000269|PubMed:8679562"
FT BINDING 408
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_04100"
FT BINDING 408
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_04100"
FT BINDING 409
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_04100"
FT BINDING 411..413
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04100"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04100"
FT BINDING 557
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04100"
FT BINDING 620
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_04100"
FT BINDING 620
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_04100"
FT SITE 618
FT /note="Optimization of metal coordination by the polymerase
FT active site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04100"
FT SITE 703
FT /note="Optimization of metal coordination by the polymerase
FT active site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04100"
FT SITE 711
FT /note="Essential for viral replication"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04100"
FT MUTAGEN 112
FT /note="D->A: Almost complete loss of exonuclease activity.
FT Decreased replication fidelity."
FT /evidence="ECO:0000269|PubMed:8262948"
FT MUTAGEN 114
FT /note="E->A: Almost complete loss of exonuclease activity.
FT Decreased replication fidelity."
FT /evidence="ECO:0000269|PubMed:8262948"
FT MUTAGEN 219
FT /note="D->A: Almost complete loss of exonuclease activity.
FT Decreased replication fidelity."
FT /evidence="ECO:0000269|PubMed:15037066,
FT ECO:0000269|PubMed:8262948"
FT MUTAGEN 324
FT /note="D->A: Almost complete loss of exonuclease activity.
FT Decreased replication fidelity."
FT /evidence="ECO:0000269|PubMed:8262948"
FT CONFLICT 89
FT /note="A -> V (in Ref. 2; CAA25344)"
FT /evidence="ECO:0000305"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1NOY"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1NOY"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:1NOY"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:1NOZ"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:1NOY"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 219..236
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1NOY"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 309..335
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:1NOY"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:1NOY"
SQ SEQUENCE 898 AA; 103610 MW; 925300C4CA5C7A24 CRC64;
MKEFYISIET VGNNIVERYI DENGKERTRE VEYLPTMFRH CKEESKYKDI YGKNCAPQKF
PSMKDARDWM KRMEDIGLEA LGMNDFKLAY ISDTYGSEIV YDRKFVRVAN CDIEVTGDKF
PDPMKAEYEI DAITHYDSID DRFYVFDLLN SMYGSVSKWD AKLAAKLDCE GGDEVPQEIL
DRVIYMPFDN ERDMLMEYIN LWEQKRPAIF TGWNIEGFDV PYIMNRVKMI LGERSMKRFS
PIGRVKSKLI QNMYGSKEIY SIDGVSILDY LDLYKKFAFT NLPSFSLESV AQHETKKGKL
PYDGPINKLR ETNHQRYISY NIIDVESVQA IDKIRGFIDL VLSMSYYAKM PFSGVMSPIK
TWDAIIFNSL KGEHKVIPQQ GSHVKQSFPG AFVFEPKPIA RRYIMSFDLT SLYPSIIRQV
NISPETIRGQ FKVHPIHEYI AGTAPKPSDE YSCSPNGWMY DKHQEGIIPK EIAKVFFQRK
DWKKKMFAEE MNAEAIKKII MKGAGSCSTK PEVERYVKFS DDFLNELSNY TESVLNSLIE
ECEKAATLAN TNQLNRKILI NSLYGALGNI HFRYYDLRNA TAITIFGQVG IQWIARKINE
YLNKVCGTND EDFIAAGDTD SVYVCVDKVI EKVGLDRFKE QNDLVEFMNQ FGKKKMEPMI
DVAYRELCDY MNNREHLMHM DREAISCPPL GSKGVGGFWK AKKRYALNVY DMEDKRFAEP
HLKIMGMETQ QSSTPKAVQE ALEESIRRIL QEGEESVQEY YKNFEKEYRQ LDYKVIAEVK
TANDIAKYDD KGWPGFKCPF HIRGVLTYRR AVSGLGVAPI LDGNKVMVLP LREGNPFGDK
CIAWPSGTEL PKEIRSDVLS WIDHSTLFQK SFVKPLAGMC ESAGMDYEEK ASLDFLFG
