DPOE1_DROME
ID DPOE1_DROME Reviewed; 2236 AA.
AC Q9VCN1; Q95R46;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=DNA polymerase epsilon catalytic subunit 1 {ECO:0000305};
DE EC=2.7.7.7 {ECO:0000269|PubMed:15135399};
DE AltName: Full=3'-5' exodeoxyribonuclease {ECO:0000305};
DE EC=3.1.11.- {ECO:0000269|PubMed:15135399};
DE AltName: Full=DNA polymerase epsilon 255kD subunit {ECO:0000303|PubMed:22245183};
DE AltName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000255|RuleBase:RU365029};
DE AltName: Full=DNA polymerase epsilon subunit 1 {ECO:0000312|FlyBase:FBgn0264326};
GN Name=PolE1 {ECO:0000312|FlyBase:FBgn0264326};
GN Synonyms=DNApol-epsilon {ECO:0000312|FlyBase:FBgn0264326},
GN DNApol-epsilon255 {ECO:0000303|PubMed:22245183},
GN l(3)pl10 {ECO:0000303|PubMed:21898761, ECO:0000312|FlyBase:FBgn0264326},
GN l(3)pl10R {ECO:0000312|FlyBase:FBgn0264326},
GN Polepsilon {ECO:0000312|FlyBase:FBgn0264326};
GN ORFNames=CG6768 {ECO:0000312|FlyBase:FBgn0264326};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL29168.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1519-2236.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL29168.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL29168.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=11054539; DOI=10.1016/s0378-1119(00)00370-x;
RA Oshige M., Yoshida H., Hirose F., Takata K.I., Inoue Y., Aoyagi N.,
RA Yamaguchi M., Koiwai O., Matsukage A., Sakaguchi K.;
RT "Molecular cloning and expression during development of the Drosophila gene
RT for the catalytic subunit of DNA polymerase epsilon.";
RL Gene 256:93-100(2000).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DEVELOPMENTAL STAGE.
RX PubMed=15135399; DOI=10.1016/j.pep.2004.02.001;
RA Oshige M., Takeuchi R., Ruike T., Ruike R., Kuroda K., Sakaguchi K.;
RT "Subunit protein-affinity isolation of Drosophila DNA polymerase catalytic
RT subunit.";
RL Protein Expr. Purif. 35:248-256(2004).
RN [6] {ECO:0000305}
RP FUNCTION, DOMAIN, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22245183; DOI=10.1016/j.gene.2011.12.056;
RA Suyari O., Kawai M., Ida H., Yoshida H., Sakaguchi K., Yamaguchi M.;
RT "Differential requirement for the N-terminal catalytic domain of the DNA
RT polymerase epsilon p255 subunit in the mitotic cell cycle and the
RT endocycle.";
RL Gene 495:104-114(2012).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=21898761; DOI=10.1002/dvg.20791;
RA Verma A., Sengupta S., Lakhotia S.C.;
RT "DNApol-epsilon gene is indispensable for the survival and growth of
RT Drosophila melanogaster.";
RL Genesis 50:86-101(2012).
CC -!- FUNCTION: Catalytic component of the DNA polymerase epsilon complex
CC (PubMed:15135399). Participates in chromosomal DNA replication
CC (PubMed:15135399). Required during synthesis of the leading DNA strands
CC at the replication fork, binds at/or near replication origins and moves
CC along DNA with the replication fork (By similarity). Has 3'-5'
CC proofreading exonuclease activity that corrects errors arising during
CC DNA replication (PubMed:15135399). Has a role in the G1-S transition
CC and/or S-phase progression of the mitotic cycle and endocycle
CC progression (PubMed:11054539, PubMed:15135399, PubMed:21898761).
CC Involved in DNA synthesis during DNA repair (By similarity). Plays
CC roles in larval tissue development (PubMed:22245183, PubMed:21898761).
CC {ECO:0000250|UniProtKB:P21951, ECO:0000250|UniProtKB:Q07864,
CC ECO:0000269|PubMed:11054539, ECO:0000269|PubMed:15135399,
CC ECO:0000269|PubMed:21898761, ECO:0000269|PubMed:22245183}.
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;
CC Evidence={ECO:0000269|PubMed:15135399};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22509;
CC Evidence={ECO:0000269|PubMed:15135399};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P21951};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15135399};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15135399};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P21951};
CC -!- ACTIVITY REGULATION: Inhibited by the small molecule aphidicolin
CC (PubMed:15135399). Activity is markedly inhibited by manganese ions
CC (PubMed:15135399). {ECO:0000269|PubMed:15135399}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:15135399};
CC -!- SUBUNIT: Component of the DNA polymerase epsilon complex consisting of
CC four subunits: the catalytic subunit PolE1/DNApol-epsilon255 and the
CC accessory subunits PolE2/DNApol-epsilon58, Chrac-14/DNApolE3 and PolE4.
CC {ECO:0000250|UniProtKB:Q07864}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU365029}.
CC -!- TISSUE SPECIFICITY: Expressed in salivary glands (at protein level).
CC {ECO:0000269|PubMed:22245183}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (at protein level)
CC (PubMed:11054539). Expressed at various developmental stages
CC (PubMed:11054539). {ECO:0000269|PubMed:11054539}.
CC -!- DOMAIN: The DNA polymerase activity domain resides in the N-terminal
CC half of the protein, while the C-terminus is necessary for maintenance
CC of the complex. {ECO:0000250|UniProtKB:P21951}.
CC -!- DOMAIN: The C-terminal domain (1001-2236 aa) is required for mitotic
CC DNA replication in the eye but not for DNA endoreplication in salivary
CC glands. {ECO:0000269|PubMed:22245183}.
CC -!- DOMAIN: The CysA-type zinc finger is required for PCNA-binding.
CC {ECO:0000250|UniProtKB:P15436}.
CC -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC formation of polymerase complexes. {ECO:0000250|UniProtKB:P15436}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the eye disks induces
CC a small eye phenotype and inhibits DNA synthesis (PubMed:22245183).
CC RNAi-mediated knockdown in the salivary glands results in a reduction
CC of salivary glands size together with decreased number and size of
CC nuclei in the tissue (PubMed:22245183). Also causes endoreplication
CC defects (PubMed:22245183). {ECO:0000269|PubMed:22245183}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000255|RuleBase:RU365029}.
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DR EMBL; AE014297; AAF56126.3; -; Genomic_DNA.
DR EMBL; AY061620; AAL29168.1; -; mRNA.
DR RefSeq; NP_524462.2; NM_079738.3.
DR AlphaFoldDB; Q9VCN1; -.
DR SMR; Q9VCN1; -.
DR IntAct; Q9VCN1; 7.
DR STRING; 7227.FBpp0083800; -.
DR PaxDb; Q9VCN1; -.
DR EnsemblMetazoa; FBtr0084408; FBpp0083800; FBgn0264326.
DR GeneID; 42758; -.
DR KEGG; dme:Dmel_CG6768; -.
DR CTD; 42758; -.
DR FlyBase; FBgn0264326; PolE1.
DR VEuPathDB; VectorBase:FBgn0264326; -.
DR eggNOG; KOG1798; Eukaryota.
DR GeneTree; ENSGT00390000010194; -.
DR HOGENOM; CLU_000556_0_0_1; -.
DR InParanoid; Q9VCN1; -.
DR OMA; MLDQCRY; -.
DR OrthoDB; 39650at2759; -.
DR PhylomeDB; Q9VCN1; -.
DR Reactome; R-DME-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-DME-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-DME-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-DME-5696400; Dual Incision in GG-NER.
DR Reactome; R-DME-6782135; Dual incision in TC-NER.
DR Reactome; R-DME-68952; DNA replication initiation.
DR Reactome; R-DME-68962; Activation of the pre-replicative complex.
DR SignaLink; Q9VCN1; -.
DR BioGRID-ORCS; 42758; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42758; -.
DR PRO; PR:Q9VCN1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0264326; Expressed in eye disc (Drosophila) and 14 other tissues.
DR ExpressionAtlas; Q9VCN1; baseline and differential.
DR Genevisible; Q9VCN1; DM.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IPI:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IDA:FlyBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:FlyBase.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006287; P:base-excision repair, gap-filling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IMP:FlyBase.
DR GO; GO:0045004; P:DNA replication proofreading; IDA:FlyBase.
DR GO; GO:0090592; P:DNA synthesis involved in DNA replication; IDA:FlyBase.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:FlyBase.
DR GO; GO:0007113; P:endomitotic cell cycle; IMP:FlyBase.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
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; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR013697; DNA_pol_e_suA_C.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR029703; POL2.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10670; PTHR10670; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08490; DUF1744; 1.
DR SMART; SM01159; DUF1744; 1.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Hydrolase; Iron; Iron-sulfur; Metal-binding; Nucleotidyltransferase;
KW Nucleus; Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..2236
FT /note="DNA polymerase epsilon catalytic subunit 1"
FT /id="PRO_0000448258"
FT ZN_FING 2113..2144
FT /note="CysA-type"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT REGION 1279..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1949..1985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2175..2192
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT COMPBIAS 1279..1298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1957..1985
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2178
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2190
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT CONFLICT 1616
FT /note="E -> Q (in Ref. 3; AAL29168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2236 AA; 256702 MW; D21E00C08EF8A6DD CRC64;
MSDSSKGKVL QNTGKFVSEN RTEGDDFFNE AGYRQSREND KIDSKYGFDR VKDSQERTGY
LINMHSNEVL DEDRRLIAAL DLFFIQMDGS RFKCTVAYQP YLLIRPEDNM HLEVARFLGR
KYSGQISGLE HITKEDLDLP NHLSGLQQQY IKLSFLNQTA MTKVRRELMS AVKRNQERQK
SNTYYMQMLA TSLAQSSAGS EDATLGKRQQ DYMDCIVDIR EHDVPYHVRV SIDLRIFCGQ
WYNIRCRSGV ELPTITCRPD ILDRPEPVVL AFDIETTKLP LKFPDAQTDQ VMMISYMIDG
QGYLITNREI ISSNVDDFEY TPKPEFEGNF IVFNEENEMQ LLQRFFDHIM EVRPHIIVTY
NGDFFDWPFV ETRAAVYDLD MKQEIGFSKL RDGNYLSRPA IHMDCLCWVK RDSYLPVGSQ
GLKAVAKAKL RYDPVELDPE DMCRMAVEQP QVLANYSVSD AVATYYLYMK YVHPFIFALN
TIIPMEPDEI LRKGSGTLCE TLLMVEAYHA QIVYPNKHQS ELNKLSNEGH VLDSETYVGG
HVEALESGVF RADIPCRFRL DPAMVKQLQE QVDAVLRHAI EVEEGIPLEK VLNLDEVRQE
IVQGLQGLHD IPNRLEQPVI YHLDVGAMYP NIILTNRLQP SAMVSDLDCA ACDFNKPGVR
CKRSMDWLWR GEMLPASRNE FQRIQQQLET EKFPPLFPGG PQRAFHELSK EDQAAYEKKR
LTDYCRKAYK KTKLTKLETR TSTICQKENS FYVDTVRAFR DRRYEYKGLT KVAKASVNAA
VASGDAAEIK AAKGREVLYD SLQLAHKCIL NSFYGYVMRR GARWHSMPMA GIVCLTGSNI
ITKAREIIER VGRPLELDTD GIWCILPGSF PQEFTIHTSH EKKKKINISY PNAVLNTMVK
DHFTNDQYHE LRKDKENNLP KYDIRDENSI FFEVDGPYLA MVLPAAKEEG KKLKKRYAVF
NFDGTLAELK GFEVKRRGEL QLIKNFQSSV FEAFLAGSTL EECYASVAKV ADYWLDVLYS
RGSNLPDSEL FELISENKSM SKKLEEYGAQ KSTSISTAKR LAEFLGEQMV KDAGLACKYI
ISKKPEGAPV TERAIPLAIF QSEPSVRRHH LRRWLKDNTM GDADIRDVLD WNYYIERLGG
TIQKIITIPA ALQGLANPVP RVQHPDWLHK KMLEKNDVLK QRRINEMFTS RPKPKPLATE
EDKLADMEDL AGKDGGEGAA GCPIVTKRKR IQLEEHDDEE AQPQATTWRQ ALGAPPPIGE
TRKTIVEWVR FQKKKWKWQQ DQRQRNRQAS KRTRGEDPPV VRATGSTATL GGFLRRAQRT
LLDQPWQIVQ LVPVDDLGHF TVWALIGEEL HKIKLTVPRI FYVNQRSAAP PEEGQLWRKV
NRVLPRSRPV FNLYRYSVPE QLFRDNSLGM LADLATPDIE GIYETQMTLE FRALMDMGCI
CGVQREEARR LAQLATKDLE TFSIEQLEQR PQTQVKYLAS ANNRLRKIYL YQHNTPTAKK
EIWSLILMPS KKAFVFALDT VRANQMPNMR QLYTAERLAL LKNLTAEEQD KIPVEDYTFE
VLIEVDVKQI YRHIQRALTT YKQEHQGPTI LCLQTALSAR KLSLAMPILL EFPQAEIHIS
DDASLLSGLD WQRQGSRAVI RHFLNLNNVL DLMLDQCRYF HVPIGNMPPD TVLFGADLFF
ARLLQRHNFV LWWSASTRPD LGGREADDSR LLAEFEESIS VVQNKAGFYP DVCVELALDS
LAVSALLQST RIQEMEGASS AITFDVMPQV SLEEMIGTVP AATLPSYDET ALCSAAFRVM
RSMVNGWLRE VSINRNIFSD FQIVHFYRWV RSSNALLYDP ALRRSLNNLM RKMFLRIIAE
FKRLGATIIY ADFNRIILSS GKKTVSDALG YVDYIVQSLR NKEMFHSIQL SFEQCWNFML
WMDQANFSGI RGKLPKGIDE TVSSIVSTTM IRDSERNQDD DEDEEEDSEN RDPVESNEAE
QDQEDELSLE LNWTIGEHLP DENECREKFE SLLTLFMQSL AEKKTTEQAI KDISHCAFDF
ILKLHKNYGK GKPSPGLELI RTLIKALSVD KTLAEQINEL RRNMLRLVGI GEFSDLAEWE
DPCDSHIINE VICKACNHCR DLDLCKDKHR AMKDGVPVWL CAQCYVAYDN EEIEMRMLDA
LQRKMMSYVL QDLRCSRCSE IKRENLAEFC TCAGNFVPLI SGKDIQTLLG TFNKVAANHK
MQLLQQTVHQ ALTTPR
