DPOZ_DROME
ID DPOZ_DROME Reviewed; 2130 AA.
AC Q9GSR1; Q95TM2; Q9GSR2; Q9V319;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=DNA polymerase zeta catalytic subunit {ECO:0000312|FlyBase:FBgn0002891};
DE EC=2.7.7.7 {ECO:0000269|PubMed:15175013};
GN Name=PolZ1 {ECO:0000312|FlyBase:FBgn0002891};
GN Synonyms=Dmpolzeta {ECO:0000312|EMBL:AAF59191.2},
GN DNApol-zeta {ECO:0000305}, DNApolZ1 {ECO:0000305},
GN mus205 {ECO:0000303|PubMed:11267835}, rev3 {ECO:0000303|PubMed:22532806};
GN ORFNames=CG1925 {ECO:0000312|FlyBase:FBgn0002891};
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|EMBL:AAG30223.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF 16-LEU--GLY-2130.
RX PubMed=11267835; DOI=10.1016/s0921-8777(01)00062-3;
RA Eeken J.C., Romeijn R.J., de Jong A.W., Pastink A., Lohman P.H.;
RT "Isolation and genetic characterisation of the Drosophila homologue of
RT (SCE)REV3, encoding the catalytic subunit of DNA polymerase zeta.";
RL Mutat. Res. 485:237-253(2001).
RN [2] {ECO:0000312|Proteomes:UP000000803}
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] {ECO:0000312|Proteomes:UP000000803}
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] {ECO:0000312|EMBL:AAL13918.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 739-2130.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL13918.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Farfan D., Frise E., George R., Gonzalez M.,
RA Guarin H., Li P., Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J.,
RA Paragas V., Park S., Phouanenavong S., Wan K., Yu C., Lewis S.E.,
RA Rubin G.M., Celniker S.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, IDENTIFICATION IN THE
RP DNA POLYMERASE ZETA COMPLEX, AND DEVELOPMENTAL STAGE.
RX PubMed=15175013; DOI=10.1042/bj20031833;
RA Takeuchi R., Oshige M., Uchida M., Ishikawa G., Takata K., Shimanouchi K.,
RA Kanai Y., Ruike T., Morioka H., Sakaguchi K.;
RT "Purification of Drosophila DNA polymerase zeta by REV1 protein-affinity
RT chromatography.";
RL Biochem. J. 382:535-543(2004).
RN [6] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE DNA POLYMERASE ZETA COMPLEX, INTERACTION
RP WITH RRP1, AND DEVELOPMENTAL STAGE.
RX PubMed=16507570; DOI=10.1074/jbc.m512959200;
RA Takeuchi R., Ruike T., Nakamura R., Shimanouchi K., Kanai Y., Abe Y.,
RA Ihara A., Sakaguchi K.;
RT "Drosophila DNA polymerase zeta interacts with recombination repair protein
RT 1, the Drosophila homologue of human abasic endonuclease 1.";
RL J. Biol. Chem. 281:11577-11585(2006).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=22532806; DOI=10.1371/journal.pgen.1002659;
RA Kane D.P., Shusterman M., Rong Y., McVey M.;
RT "Competition between replicative and translesion polymerases during
RT homologous recombination repair in Drosophila.";
RL PLoS Genet. 8:E1002659-E1002659(2012).
CC -!- FUNCTION: As the catalytic subunit of the DNA polymerase zeta complex,
CC plays a crucial role in translesion DNA synthesis (TLS) and various DNA
CC repair mechanisms (PubMed:11267835, PubMed:16507570, PubMed:22532806,
CC PubMed:15175013). Lacks an intrinsic 3'-5' exonuclease activity and
CC thus has no proofreading function (PubMed:15175013). During homologous
CC recombination (HR) repair, has a overlapping role with the error-prone
CC translesion polymerase eta to initiate repair synthesis which is
CC completed by end joining or another polymerase that can bind and
CC reinitiate synthesis (PubMed:22532806). May participate in the Rrp1-
CC dependent base excision repair (BER) pathway responsible for repair of
CC DNA lesions that gives rise to apurinic/apyrimidinic (AP) sites
CC (PubMed:16507570). Unlike mammalian orthologs, it is not an error-prone
CC polymerase (PubMed:15175013). {ECO:0000269|PubMed:11267835,
CC ECO:0000269|PubMed:15175013, ECO:0000269|PubMed:16507570,
CC ECO:0000269|PubMed:22532806}.
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:15175013};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P14284};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P14284};
CC -!- ACTIVITY REGULATION: Inhibited by tetracyclic diterpene antibiotic
CC aphidicolin. {ECO:0000269|PubMed:15175013}.
CC -!- SUBUNIT: Catalytic subunit of the zeta DNA polymerase complex, which
CC consists of PolZ1/DNApol-zeta and the accessory component PolZ2/Rev7
CC (PubMed:16507570, PubMed:15175013). Interacts with the
CC apurinic/apyrimidinic (AP) endonuclease Rrp1; the interaction is likely
CC indirect and mediated via PolZ2 (PubMed:16507570).
CC {ECO:0000269|PubMed:15175013, ECO:0000269|PubMed:16507570}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (at protein level)
CC (PubMed:15175013). Expressed throughout development, with highest
CC levels of expression in 0-8 hour embryos and adult females
CC (PubMed:16507570). {ECO:0000269|PubMed:15175013,
CC ECO:0000269|PubMed:16507570}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; AF298215; AAG30223.1; -; mRNA.
DR EMBL; AE013599; AAF59191.2; -; Genomic_DNA.
DR EMBL; AF298216; AAG30224.1; -; Genomic_DNA.
DR EMBL; AY058689; AAL13918.1; -; mRNA.
DR RefSeq; NP_524881.2; NM_080142.3.
DR AlphaFoldDB; Q9GSR1; -.
DR SMR; Q9GSR1; -.
DR IntAct; Q9GSR1; 1.
DR STRING; 7227.FBpp0087907; -.
DR PaxDb; Q9GSR1; -.
DR EnsemblMetazoa; FBtr0088831; FBpp0087907; FBgn0002891.
DR GeneID; 47186; -.
DR KEGG; dme:Dmel_CG1925; -.
DR UCSC; CG1925-RA; d. melanogaster.
DR CTD; 47186; -.
DR FlyBase; FBgn0002891; PolZ1.
DR VEuPathDB; VectorBase:FBgn0002891; -.
DR eggNOG; KOG0968; Eukaryota.
DR GeneTree; ENSGT00940000169521; -.
DR HOGENOM; CLU_000203_3_1_1; -.
DR InParanoid; Q9GSR1; -.
DR OMA; CYSELRG; -.
DR OrthoDB; 20210at2759; -.
DR PhylomeDB; Q9GSR1; -.
DR Reactome; R-DME-110312; Translesion synthesis by REV1.
DR Reactome; R-DME-5655862; Translesion synthesis by POLK.
DR Reactome; R-DME-5656121; Translesion synthesis by POLI.
DR BioGRID-ORCS; 47186; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 47186; -.
DR PRO; PR:Q9GSR1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0002891; Expressed in cleaving embryo and 20 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IPI:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:FlyBase.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
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:0043150; P:DNA synthesis involved in double-strand break repair via homologous recombination; IMP:FlyBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
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; 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; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR030559; PolZ_Rev3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR025687; Znf-C4pol.
DR PANTHER; PTHR45812; PTHR45812; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 2.
DR Pfam; PF14260; zf-C4pol; 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 DNA damage; DNA repair; DNA synthesis; DNA-directed DNA polymerase; Iron;
KW Iron-sulfur; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase; Zinc.
FT CHAIN 1..2130
FT /note="DNA polymerase zeta catalytic subunit"
FT /id="PRO_0000448742"
FT REGION 528..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2086..2103
FT /note="CysB motif"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT COMPBIAS 553..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1222..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2041
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2045
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2054
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2057
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2086
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2089
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2098
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT BINDING 2103
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P15436"
FT MUTAGEN 14..2130
FT /note="Missing: In mus205; hypersensitive to alkylating
FT agents and UV, but not sensitive to ionising radiation. In
FT somatic cells, no effect on methyl methane sulfonate-
FT induced mutations and homologous recombination. In germ
FT cells, no effect on mutability by X-rays, NQO and
FT alkylating agents."
FT /evidence="ECO:0000269|PubMed:11267835"
FT CONFLICT 92
FT /note="M -> V (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="A -> V (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="S -> N (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="A -> V (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="R -> H (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="S -> R (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 854
FT /note="C -> R (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="C -> S (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="D -> G (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 1176
FT /note="E -> D (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 1206
FT /note="T -> R (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 1213
FT /note="R -> P (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 1238
FT /note="S -> F (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 1524
FT /note="D -> E (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 1611
FT /note="Y -> H (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 1852
FT /note="V -> E (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
FT CONFLICT 2025
FT /note="A -> P (in Ref. 1; AAG30223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2130 AA; 240073 MW; 24686E9A2267FC15 CRC64;
MAAAGEAIDG VYSVRLVIAD FYMEKPQFGM DPCYSELRGK EIKRVPVIRV FGGNSRGQKT
CMHVHGVFPY LYIPYDKKDF ESLERGILQM AMHLDKAINI SLGQGSSNAQ HVFKIQLVKG
IPFYGYHRVE HQFLKIYMFN PRFVRRAANL LQSGAILSKN FSPHESHVPY ILQFMIDYNL
YGMSYVHVPL EVLKFRRNHD DDVIPYANVK QAQLLDITTA KKVACSALEV DVSSNFILNR
FQLVAKSKSN HTNPGIEAIW NDEKLRRQKL VEKHTDAGDE EKAEAVPVLE LPPTQERHQI
EIAESDIFYR TALESKLMTL EQSTLSEQTL SDQTILPQAT MQTTMPGTKA QKRRFNLQKL
LANAVYPEEC SQDQQQLLVN ASFIQNHVTC GYSSSVSLST SKDESDDLDE TVVDEELILS
LTQPHGAIPH DATLREEDLE LLDALQLLEE QNESESHVDL DSSLAPLSQH KKFELTPELL
DKETAATAAL FDEDVDSDED ADQETRHDFS TVLDDVDELL LKLTQSQPAE SKELKASSKL
PQIDGADDRL QRTPIKSISS KSKSSPSKTP TTPIGQKSLP KSPRTPKTSA AKKYAPLALT
IGSSSSKKSN DEFAGRPSNP RLSLQLDQGT GTGTLRPEIS LRKKLAMSEM RRKSFEDSFV
LLKNDCTPVR STRRSTSNLD KTHIICSLTP RDRNPGLSDM FETEDGKQLP PKKVVRKTRW
STRNQDIESL PKAGCEIERP HRSEGSALDE LKPRRSARHK VNSANPDECS SEIQTTGPRV
TTTSLDRPQK KARLSQSPKE NTKTSMNGTV ALEKATKDSS SNSESPHQQE NSVSEQIEYL
ESKPKKSDET ARSCDEKLQR ELIPQEPAGI SPGDSANSTE EITFSPCHDE AIESDTESDY
IVTKLRKTPN LKRLRWSIRS ELLNKQFTPS SGIRPPETET TPQLSPKSNE SNTPELMRSF
YEHSLIVNSP SVFSDFLDSP EIHMDSPRSA PPSPDSNSFV IAPLELPPSY DEVVSGSRKM
DIPEYEFQKP YYSNPSDVSK VTEVGFLVLH IPGNKLNDCD PFQSILGNDR GLASWRRRQL
IAIGGLAMLQ RHRGEQKVRE YFSTQQRIAI EPAQLAPTWQ EAKIWLKAKE LLRQREEPKK
SSDDIDSPIK IKRQKITMML QAEEGDGGSG DEDAGEELDC SLSLTPLSQA KDKCKATPTS
SKARETGKSR LKRGTRLSFI GSQDEEPPSS QSSEQSVSSS AAQAELDRSS FLRQLEGSSQ
DRQHDLSFGL SHATLDNTFG FKVNLENLQQ AKADIDCNHL TIITLEVFVS TRGDLQPDPM
HDEIRCLFYA IEHSLPDEKL PSKACGYIMV NTVQDLLSEG PFHGIDRDIE VQVVTSEAEA
FEALLALCER WDADIYAGYE IEMSSWGYVI DRAKHLCFNI APLLSRVPTQ KVRDFVDEDR
EQFTDLDVEM KLCGRILLDV WRLMRSEIAL TSYTFENVMY HILHKRCPWH TAKSLTEWFG
SPCTRWIVME YYLERVRGTL TLLDQLDLLG RTSEMAKLIG IQFYEVLSRG SQFRVESMML
RIAKPKNLVP LSPSVQARAH MRAPEYLALI MEPQSRFYAD PLIVLDFQSL YPSMIIAYNY
CFSTCLGRVE HLGGSSPFEF GASQLRVSRQ MLQKLLEHDL VTVSPCGVVF VKREVREGIL
PRMLTEILDT RQMVKQSMKL HKDSSALQRI LHSRQLGLKL MANVTYGYTA ANFSGRMPSV
EVGDSVVSKG RETLERAIKL VENNEEWKVR VVYGDTDSMF VLVPGRNRAE AFRIGEEIAK
AVTEMNPQPV KLKLEKVYQP CMLQTKKRYV GYMYETADQE QPVYEAKGIE TVRRDGCPAV
AKMLEKVLRI LFETQDVSKI KAYVCRQFTK LLSGRANLQD LIFAKEFRGL NGYKPTACVP
ALELTRKWMQ KDPRHVPRRG ERVPFIIVNG PPGMQLIRLV RSPHDILANE GHKINAIYYI
TKAIIPPLNR CLLLIGANVH DWFASLPRKL LMTPAVGTAN ELAGARGAKS TISQYFSTTS
CVIDCGRQTK AGICPDCLKN ATTCVVVLSD KTARLERGYQ LTRQICQACC GRLGSLQCDS
LDCPVLYVLE GKRRELQQIE HWNKLLEHHF
