DPOLQ_DROME
ID DPOLQ_DROME Reviewed; 2059 AA.
AC O18475; Q5BI65;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=DNA polymerase theta {ECO:0000303|PubMed:20617203};
DE EC=2.7.7.7 {ECO:0000269|PubMed:10343651, ECO:0000269|PubMed:15961355, ECO:0000269|PubMed:28542210};
DE AltName: Full=Mutagen-sensitive protein 308 {ECO:0000303|PubMed:8816490};
GN Name=PolQ {ECO:0000312|FlyBase:FBgn0002905};
GN Synonyms=DNApol-theta {ECO:0000303|PubMed:8816490}, DNApolQ {ECO:0000305},
GN mus308 {ECO:0000303|PubMed:8816490, ECO:0000312|FlyBase:FBgn0002905};
GN ORFNames=CG6019 {ECO:0000312|FlyBase:FBgn0002905};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=Iso-1;
RX PubMed=8816490; DOI=10.1128/mcb.16.10.5764;
RA Harris P.V., Mazina O.M., Leonhardt E.A., Case R.B., Boyd J.B.,
RA Burtis K.C.;
RT "Molecular cloning of Drosophila mus308, a gene involved in DNA cross-link
RT repair with homology to prokaryotic DNA polymerase I genes.";
RL Mol. Cell. Biol. 16:5764-5771(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10343651; DOI=10.1016/s0921-8777(99)00005-1;
RA Oshige M., Aoyagi N., Harris P.V., Burtis K.C., Sakaguchi K.;
RT "A new DNA polymerase species from Drosophila melanogaster: a probable
RT mus308 gene product.";
RL Mutat. Res. 433:183-192(1999).
RN [6]
RP FUNCTION.
RX PubMed=10732683; DOI=10.1007/s004380050041;
RA Tosal L., Comendador M.A., Sierra L.M.;
RT "The mus308 locus of Drosophila melanogaster is implicated in the bypass of
RT ENU-induced O-alkylpyrimidine adducts.";
RL Mol. Gen. Genet. 263:144-151(2000).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=15961355; DOI=10.1016/j.dnarep.2005.04.020;
RA Pang M., McConnell M., Fisher P.A.;
RT "The Drosophila mus 308 gene product, implicated in tolerance of DNA
RT interstrand crosslinks, is a nuclear protein found in both ovaries and
RT embryos.";
RL DNA Repair 4:971-982(2005).
RN [8]
RP FUNCTION.
RX PubMed=20936147; DOI=10.4061/2010/416364;
RA Diaz-Valdes N., Comendador M.A., Sierra L.M.;
RT "Mus308 processes oxygen and nitrogen ethylation DNA damage in germ cells
RT of Drosophila.";
RL J. Nucleic Acids 2010:H1947-1958(2010).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLY-621 AND PRO-781.
RX PubMed=20617203; DOI=10.1371/journal.pgen.1001005;
RA Chan S.H., Yu A.M., McVey M.;
RT "Dual roles for DNA polymerase theta in alternative end-joining repair of
RT double-strand breaks in Drosophila.";
RL PLoS Genet. 6:E1001005-E1001005(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27849606; DOI=10.1073/pnas.1617110113;
RA Alexander J.L., Beagan K., Orr-Weaver T.L., McVey M.;
RT "Multiple mechanisms contribute to double-strand break repair at
RT rereplication forks in Drosophila follicle cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:13809-13814(2016).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-262 AND
RP 1825-ASP-PHE-1826.
RX PubMed=28542210; DOI=10.1371/journal.pgen.1006813;
RA Beagan K., Armstrong R.L., Witsell A., Roy U., Renedo N., Baker A.E.,
RA Schaerer O.D., McVey M.;
RT "Drosophila DNA polymerase theta utilizes both helicase-like and polymerase
RT domains during microhomology-mediated end joining and interstrand crosslink
RT repair.";
RL PLoS Genet. 13:E1006813-E1006813(2017).
CC -!- FUNCTION: Multifunctional protein with both DNA polymerase and ATPase
CC activities (PubMed:10343651, PubMed:15961355). Might have 3' to 5'
CC exonuclease activity (PubMed:10343651). Plays a role in different DNA
CC repair pathways such as DNA strand cross-link repair and microhomology-
CC mediated end-joining (MMEJ), an alternative non-homologous end-joining
CC (NHEJ) machinery triggered in response to double-strand breaks
CC (PubMed:20936147, PubMed:20617203, PubMed:28542210). MMEJ is an error-
CC prone repair pathway that produces deletions of sequences from the
CC strand being repaired and promotes genomic rearrangements, such as
CC telomere fusions (PubMed:20617203). Utilizes short microhomologies
CC present in partially and fully single-stranded DNA (ssDNA) as primers
CC for DNA synthesis (PubMed:28542210). Prefers poly(dA)/oligo(dT) as a
CC template-primer (PubMed:10343651). The ATPase activity is necessary
CC during interstrand cross-link (ICL) repair and has a critical role in
CC generating templated insertions during MMEJ (PubMed:28542210).
CC Necessary for processing DNA damage induced by oxygen and N-ethylation
CC (PubMed:10732683, PubMed:20936147). In follicle cells, contributes to
CC double-strand break repair at physiological rereplication forks
CC necessary for survival of fertilized eggs (PubMed:20936147,
CC PubMed:27849606). {ECO:0000269|PubMed:10343651,
CC ECO:0000269|PubMed:10732683, ECO:0000269|PubMed:15961355,
CC ECO:0000269|PubMed:20617203, ECO:0000269|PubMed:20936147,
CC ECO:0000269|PubMed:27849606, ECO:0000269|PubMed:28542210}.
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:10343651, ECO:0000269|PubMed:15961355,
CC ECO:0000269|PubMed:28542210};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10343651};
CC -!- ACTIVITY REGULATION: Resistant to aphidicolin, but sensitive to
CC dideoxythymindine triphosphate (ddTTP) and N-ethyl malemide (NEM).
CC {ECO:0000269|PubMed:10343651, ECO:0000269|PubMed:15961355}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:10343651};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15961355}.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries (at protein level).
CC {ECO:0000269|PubMed:15961355}.
CC -!- DEVELOPMENTAL STAGE: Expressed from before hatching of first instar
CC larvae (at protein level). {ECO:0000269|PubMed:15961355}.
CC -!- PTM: In adult males, cleaved to produce a 100 kDa form.
CC {ECO:0000269|PubMed:15961355}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to DNA-cross-linking agents
CC (PubMed:8816490). In follicle cells, results in reduced fork
CC progression in physiological rereplication regions necessary for the
CC amplification of the eggshell (chorion) protein genes
CC (PubMed:27849606). Reduces mRNA expression of chorion protein genes
CC which results in compromised eggshell integrity and reduced egg
CC hatching frequency (PubMed:27849606). In follicle cells, simultaneous
CC knockout of DNAlig4 and DNApol-theta reduces rereplication origin
CC firing (PubMed:27849606). {ECO:0000269|PubMed:27849606,
CC ECO:0000269|PubMed:8816490}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR EMBL; L76559; AAB67306.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54858.1; -; Genomic_DNA.
DR EMBL; BT021359; AAX33507.1; -; mRNA.
DR EMBL; BT044169; ACH92234.1; -; mRNA.
DR PIR; T13858; T13858.
DR RefSeq; NP_524333.1; NM_079609.3.
DR AlphaFoldDB; O18475; -.
DR SMR; O18475; -.
DR IntAct; O18475; 4.
DR STRING; 7227.FBpp0082131; -.
DR PaxDb; O18475; -.
DR PRIDE; O18475; -.
DR EnsemblMetazoa; FBtr0082662; FBpp0082131; FBgn0002905.
DR GeneID; 41571; -.
DR KEGG; dme:Dmel_CG6019; -.
DR UCSC; CG6019-RA; d. melanogaster.
DR CTD; 41571; -.
DR FlyBase; FBgn0002905; PolQ.
DR VEuPathDB; VectorBase:FBgn0002905; -.
DR eggNOG; KOG0950; Eukaryota.
DR GeneTree; ENSGT00940000158694; -.
DR HOGENOM; CLU_000818_0_0_1; -.
DR InParanoid; O18475; -.
DR OMA; NVSFCAE; -.
DR OrthoDB; 179246at2759; -.
DR PhylomeDB; O18475; -.
DR Reactome; R-DME-5685939; HDR through MMEJ (alt-NHEJ).
DR SignaLink; O18475; -.
DR BioGRID-ORCS; 41571; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41571; -.
DR PRO; PR:O18475; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002905; Expressed in gastrula and 30 other tissues.
DR Genevisible; O18475; DM.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:FlyBase.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISS:FlyBase.
DR GO; GO:0071897; P:DNA biosynthetic process; IDA:FlyBase.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IDA:FlyBase.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IMP:UniProtKB.
DR GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IMP:FlyBase.
DR GO; GO:0031297; P:replication fork processing; IGI:UniProtKB.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10133; PTHR10133; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-directed DNA polymerase;
KW Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..2059
FT /note="DNA polymerase theta"
FT /id="PRO_0000432704"
FT DOMAIN 243..416
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 464..666
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 25..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 357..360
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 28..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 256..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 262
FT /note="K->A: Increases sensitivity to DNA interstrand
FT damage induced by DNA-cross-linking agents. Reduces
FT annealing and extension of single-strand DNA molecules in
FT vitro but does not affect end-joining frequency."
FT /evidence="ECO:0000269|PubMed:28542210"
FT MUTAGEN 621
FT /note="G->S: In mus308(3294); flies are unable to repair
FT interstrand cross-links."
FT /evidence="ECO:0000269|PubMed:20617203"
FT MUTAGEN 781
FT /note="P->L: In mus308(D5); flies are unable to repair
FT interstrand cross-links."
FT /evidence="ECO:0000269|PubMed:20617203"
FT MUTAGEN 1825..1826
FT /note="DF->AA: Increases sensitivity to DNA interstrand
FT damage induced by DNA-cross-linking agents and ionizing
FT radiation. Reduces alternative end-joining repair."
FT /evidence="ECO:0000269|PubMed:28542210"
FT CONFLICT 1930
FT /note="R -> H (in Ref. 4; AAX33507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2059 AA; 229873 MW; E93B3CD9A5F75F16 CRC64;
MAFSQSFNFG NSTLMALEKG MQADDKENAQ PGNGNIQVQS AGNEVNSEIQ EINSEFFRDE
FSYEVNQAHK PAEQSVVNVS QVQQHMAVVS NQDSEDQSRS SALNDQICTQ SSFEGEDAGA
DAVLDQPNLD ENSFLCPAQD EEASEQLKED ILHSHSVLAK QEFYQEISQV TQNLSSMSPN
QLRVSPNSSR IREAMPERPA MPLDLNTLRS ISAWNLPMSI QAEYKKKGVV DMFDWQVECL
SKPRLLFEHC NLVYSAPTSA GKTLVSEILM LKTVLERGKK VLLILPFISV VREKMFYMQD
LLTPAGYRVE GFYGGYTPPG GFESLHVAIC TIEKANSIVN KLMEQGKLET IGMVVVDEVH
LISDKGRGYI LELLLAKILY MSRRNGLQIQ VITMSATLEN VQLLQSWLDA ELYITNYRPV
ALKEMIKVGT VIYDHRLKLV RDVAKQKVLL KGLENDSDDV ALLCIETLLE GCSVIVFCPS
KDWCENLAVQ LATAIHVQIK SETVLGQRLR TNLNPRAIAE VKQQLRDIPT GLDGVMSKAI
TYACAFHHAG LTTEERDIIE ASFKAGALKV LVATSTLSSG VNLPARRVLI RSPLFGGKQM
SSLTYRQMIG RAGRMGKDTL GESILICNEI NARMGRDLVV SELQPITSCL DMDGSTHLKR
ALLEVISSGV ANTKEDIDFF VNCTLLSAQK AFHAKEKPPD EESDANYIND ALDFLVEYEF
VRLQRNEERE TAVYVATRLG AACLASSMPP TDGLILFAEL QKSRRSFVLE SELHAVYLVT
PYSVCYQLQD IDWLLYVHMW EKLSSPMKKV GELVGVRDAF LYKALRGQTK LDYKQMQIHK
RFYIALALEE LVNETPINVV VHKYKCHRGM LQSLQQMAST FAGIVTAFCN SLQWSTLALI
VSQFKDRLFF GIHRDLIDLM RIPDLSQKRA RALFDAGITS LVELAGADPV ELEKVLYNSI
SFDSAKQHDH ENADEAAKRN VVRNFYITGK AGMTVSEAAK LLIGEARQFV QHEIGLGTIK
WTQTQAGVEI ASRAIHDGGE VDLHMSLEEE QPPVKRKLSI EENGTANSQK NPRLETVVDT
QRGYKVDKNI ANQSKMNPNL KEIDAQNKAR RNSTAHMDNL NPISNDPCQN NVNVKTAQPI
ISNLNDIQKQ GSQIEKMKIN PATVVCSPQL ANEEKPSTSQ SARRKLVNEG MAERRRVALM
KIQQRTQKEN QSKDQPIQAS RSNQLSSPVN RTPANRWTQS ENPNNEMNNS QLPRRNPRNQ
SPVPNANRTA SRKVSNAEED LFMADDSFML NTGLAAALTA AESKIASCTE ADVIPSSQPK
EPEVIGALTP HASRLKRSDQ LRSQRIQSPS PTPQREIEID LESKNESNGV SSMEISDMSM
ENPLMKNPLH LNASHIMSCS KVDETASSFS SIDIIDVCGH RNAFQAAIIE INNATRLGFS
VGLQAQAGKQ KPLIGSNLLI NQVAAAENRE AAARERVLFQ VDDTNFISGV SFCLADNVAY
YWNMQIDERA AYQGVPTPLK VQELCNLMAR KDLTLVMHDG KEQLKMLRKA IPQLKRISAK
LEDAKVANWL LQPDKTVNFL NMCQTFAPEC TGLANLCGSG RGYSSYGLDT SSAILPRIRT
AIESCVTLHI LQGQTENLSR IGNGDLLKFF HDIEMPIQLT LCQMELVGFP AQKQRLQQLY
QRMVAVMKKV ETKIYEQHGS RFNLGSSQAV AKVLGLHRKA KGRVTTSRQV LEKLNSPISH
LILGYRKLSG LLAKSIQPLM ECCQADRIHG QSITYTATGR ISMTEPNLQN VAKEFSIQVG
SDVVHISCRS PFMPTDESRC LLSADFCQLE MRILAHMSQD KALLEVMKSS QDLFIAIAAH
WNKIEESEVT QDLRNSTKQV CYGIVYGMGM RSLAESLNCS EQEARMISDQ FHQAYKGIRD
YTTRVVNFAR SKGFVETITG RRRYLENINS DVEHLKNQAE RQAVNSTIQG SAADIAKNAI
LKMEKNIERY REKLALGDNS VDLVMHLHDE LIFEVPTGKA KKIAKVLSLT MENCVKLSVP
LKVKLRIGRS WGEFKEVSV
