RAD50_DROME
ID RAD50_DROME Reviewed; 1318 AA.
AC Q9W252; B6UXS6; B6UXT1; B6UXT2; B6UXT3; B6UXT4; B6UXT5; B6UXT6; B6UXT7;
AC B6UXT8; B6UXT9; B6UXU1; B6UXU2; B6UXU3; B6UXU4; B6UXU5; B6UXU6; B6UXU7;
AC B6UXU8; B6UXU9; B6UXV0; B6UXV1; B6UXV2; Q86NZ9; Q960E0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 4.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=DNA repair protein RAD50;
DE EC=3.6.-.-;
GN Name=rad50; ORFNames=CG6339;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-657, AND VARIANTS ASP-208; VAL-219;
RP GLU-220; GLU-246; MET-249; GLN-281; THR-349; GLU-422; ILE-450; ASN-480;
RP GLN-490; ILE-491; SER-580; ILE-586; ASN-623; SER-646 AND ALA-657.
RC STRAIN=MW11, MW25, MW27, MW56, MW6, MW9, NC301, NC303, NC304, NC306, NC322,
RC NC335, NC336, NC350, NC357, NC358, NC359, NC361, NC362, NC375, NC390,
RC NC397, and NC399;
RX PubMed=18984573; DOI=10.1534/genetics.108.093807;
RA Anderson J.A., Gilliland W.D., Langley C.H.;
RT "Molecular population genetics and evolution of Drosophila meiosis genes.";
RL Genetics 181:177-185(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 500-1318.
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15296753; DOI=10.1016/j.cub.2004.07.019;
RA Ciapponi L., Cenci G., Ducau J., Flores C., Johnson-Schlitz D.,
RA Gorski M.M., Engels W.R., Gatti M.;
RT "The Drosophila Mre11/Rad50 complex is required to prevent both telomeric
RT fusion and chromosome breakage.";
RL Curr. Biol. 14:1360-1366(2004).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15135728; DOI=10.1016/j.dnarep.2004.02.001;
RA Gorski M.M., Romeijn R.J., Eeken J.C.J., de Jong A.W.M., van Veen B.L.,
RA Szuhai K., Mullenders L.H., Ferro W., Pastink A.;
RT "Disruption of Drosophila Rad50 causes pupal lethality, the accumulation of
RT DNA double-strand breaks and the induction of apoptosis in third instar
RT larvae.";
RL DNA Repair 3:603-615(2004).
CC -!- FUNCTION: Essential component of the MRN complex, a complex that
CC possesses single-stranded DNA endonuclease and 3' to 5' exonuclease
CC activities, and plays a central role in double-strand break (DSB)
CC repair. The complex participates in processes such as DNA
CC recombination, DNA repair, genome stability, telomere integrity and
CC meiosis. The MRN complex may protect telomeres by facilitating
CC recruitment of HOAP and HP1 at chromosome ends. In the complex, it
CC mediates the ATP-binding and is probably required to bind DNA ends and
CC hold them in close proximity. {ECO:0000269|PubMed:15135728,
CC ECO:0000269|PubMed:15296753}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per homodimer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. Probable component of the MRN complex with mre11
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15296753}. Chromosome
CC {ECO:0000269|PubMed:15296753}. Chromosome, telomere
CC {ECO:0000269|PubMed:15296753}. Note=Uniformly distributed along mitotic
CC chromosomes.
CC -!- DOMAIN: The zinc-hook, which separates the large intramolecular coiled
CC coil regions, contains 2 Cys residues that coordinate one molecule of
CC zinc with the help of the 2 Cys residues of the zinc-hook of another
CC RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of
CC the homodimer, which constitute the ATP-binding domain, interact with
CC the MRE11 homodimer (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Death during pupal stage, possibly due to the
CC accumulation of DNA DSBs and the induction of apoptosis in third instar
CC larvae. {ECO:0000269|PubMed:15135728}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93530.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO39559.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF46847.3; -; Genomic_DNA.
DR EMBL; BT003555; AAO39559.1; ALT_INIT; mRNA.
DR EMBL; FJ219324; ACI97309.1; -; Genomic_DNA.
DR EMBL; FJ219329; ACI97314.1; -; Genomic_DNA.
DR EMBL; FJ219330; ACI97315.1; -; Genomic_DNA.
DR EMBL; FJ219331; ACI97316.1; -; Genomic_DNA.
DR EMBL; FJ219332; ACI97317.1; -; Genomic_DNA.
DR EMBL; FJ219333; ACI97318.1; -; Genomic_DNA.
DR EMBL; FJ219334; ACI97319.1; -; Genomic_DNA.
DR EMBL; FJ219335; ACI97320.1; -; Genomic_DNA.
DR EMBL; FJ219336; ACI97321.1; -; Genomic_DNA.
DR EMBL; FJ219337; ACI97322.1; -; Genomic_DNA.
DR EMBL; FJ219338; ACI97323.1; -; Genomic_DNA.
DR EMBL; FJ219339; ACI97324.1; -; Genomic_DNA.
DR EMBL; FJ219340; ACI97325.1; -; Genomic_DNA.
DR EMBL; FJ219341; ACI97326.1; -; Genomic_DNA.
DR EMBL; FJ219342; ACI97327.1; -; Genomic_DNA.
DR EMBL; FJ219343; ACI97328.1; -; Genomic_DNA.
DR EMBL; FJ219344; ACI97329.1; -; Genomic_DNA.
DR EMBL; FJ219345; ACI97330.1; -; Genomic_DNA.
DR EMBL; FJ219346; ACI97331.1; -; Genomic_DNA.
DR EMBL; FJ219347; ACI97332.1; -; Genomic_DNA.
DR EMBL; FJ219348; ACI97333.1; -; Genomic_DNA.
DR EMBL; FJ219349; ACI97334.1; -; Genomic_DNA.
DR EMBL; FJ219350; ACI97335.1; -; Genomic_DNA.
DR EMBL; AY052106; AAK93530.1; ALT_INIT; mRNA.
DR RefSeq; NP_726199.3; NM_166533.4.
DR AlphaFoldDB; Q9W252; -.
DR SMR; Q9W252; -.
DR BioGRID; 63180; 17.
DR IntAct; Q9W252; 5.
DR STRING; 7227.FBpp0290882; -.
DR PaxDb; Q9W252; -.
DR DNASU; 37564; -.
DR EnsemblMetazoa; FBtr0301668; FBpp0290882; FBgn0034728.
DR GeneID; 37564; -.
DR KEGG; dme:Dmel_CG6339; -.
DR UCSC; CG6339-RB; d. melanogaster.
DR CTD; 10111; -.
DR FlyBase; FBgn0034728; rad50.
DR VEuPathDB; VectorBase:FBgn0034728; -.
DR eggNOG; KOG0962; Eukaryota.
DR GeneTree; ENSGT00390000018781; -.
DR InParanoid; Q9W252; -.
DR OMA; CFGVNCG; -.
DR OrthoDB; 179362at2759; -.
DR PhylomeDB; Q9W252; -.
DR Reactome; R-DME-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-DME-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-DME-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DME-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-69473; G2/M DNA damage checkpoint.
DR SignaLink; Q9W252; -.
DR BioGRID-ORCS; 37564; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 37564; -.
DR PRO; PR:Q9W252; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034728; Expressed in capitellum (Drosophila) and 36 other tissues.
DR ExpressionAtlas; Q9W252; baseline and differential.
DR Genevisible; Q9W252; DM.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR GO; GO:0030870; C:Mre11 complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IMP:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IMP:FlyBase.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IMP:FlyBase.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR CDD; cd03240; ABC_Rad50; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045171; ABC_Rad50.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR004584; Rad50_eukaryotes.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR TIGRFAMs; TIGR00606; rad50; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Chromosome; Coiled coil; DNA damage; DNA repair;
KW Hydrolase; Meiosis; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Telomere; Zinc.
FT CHAIN 1..1318
FT /note="DNA repair protein RAD50"
FT /id="PRO_0000138645"
FT DOMAIN 645..741
FT /note="Zinc-hook"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT REGION 447..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 189..256
FT /evidence="ECO:0000255"
FT COILED 305..333
FT /evidence="ECO:0000255"
FT COILED 434..641
FT /evidence="ECO:0000255"
FT COILED 645..685
FT /evidence="ECO:0000255"
FT COILED 713..741
FT /evidence="ECO:0000255"
FT COILED 830..1101
FT /evidence="ECO:0000255"
FT COMPBIAS 451..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 689
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT BINDING 692
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00471"
FT VARIANT 208
FT /note="E -> D (in strain: NC335, NC362 and NC390)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 219
FT /note="H -> V (in strain: NC335, NC362 and NC390)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 220
FT /note="V -> E (in strain: NC335, NC362 and NC390)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 246
FT /note="A -> E (in strain: MW25)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 249
FT /note="S -> M (in strain: MW25)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 281
FT /note="E -> Q (in strain: NC306)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 349
FT /note="K -> T (in strain: MW9)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 422
FT /note="V -> E (in strain: NC361 and NC375)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 450
FT /note="V -> I (in strain: MW6)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 480
FT /note="D -> N (in strain: MW6)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 490
FT /note="E -> Q (in strain: MW25, MW27, MW56, MW9, NC303,
FT NC306, NC335, NC336, NC390 and NC399)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 491
FT /note="V -> I (in strain: NC303, NC306 and NC335)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 580
FT /note="C -> S (in strain: MW25)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 586
FT /note="M -> I (in strain: MW25)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 623
FT /note="S -> N (in strain: NC336, NC358, NC361, NC362 and
FT NC375)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 646
FT /note="T -> S (in strain: NC357 and NC397)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT VARIANT 657
FT /note="T -> A (in strain: MW6, NC357, NC358, NC361, NC362,
FT NC375 and NC397)"
FT /evidence="ECO:0000269|PubMed:18984573"
FT CONFLICT 880
FT /note="R -> K (in Ref. 5; AAK93530)"
FT /evidence="ECO:0000305"
FT CONFLICT 959
FT /note="H -> Q (in Ref. 5; AAK93530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1318 AA; 152160 MW; 1C84EB7B3F9E3BB9 CRC64;
MSSIESLSIQ GIRSFGTYAD DLQSIKFSSP VTLILGENGC GKTTVVECLK YALTGECPPG
SDRGKSFVHD PKIFGLNEVL AQIKMQVRDR RGAQVSICRT MKVSKKRNKM SFETMDSTIN
FLTGAGQSKR EKQDSLSGRS VDIDVAISDF MGVSKAIINN VLFCHQEDSS WPLDESKKLK
EKFDAIFGIT EYNKALDKII KLRKEAMEEL KIKEANIKHV AYLKQEMEVK TLNLQKAQRK
CDAIKAQCSE CEEEMKPIEA RLVEIRNVEF EIGKYQAQKV EMDTKHKNCK DQISTLTLKI
KKPFRGTLDE LDQEISNFDQ RMLEMRQKRT EVEGDLSQIK RSSVAEQEKL GTQDRKHCLA
KQRHQSELAC RAQLLKRVKE FCRELHIPID CDLVEQPEKM GEVLRDIEAM IITKHCEITE
IVEQNEKADR SRQVKIDELR IELTKSEQSV TAQEKQRESS KRESETLGVE IKKIETSMQD
LKKLEKEINE VNELYESATK NIDQQAIKDA IARKKASIAE NQIQFKKLDE QLTFLGSMAK
LVAECSLKQK ELDKKNQEVH RVRSRHSDHF GKLFKEPITC NYRRSMQVVY EKLRREIQEL
NEKANTQKLK EQSYEIKRKN LISDISRMEK ELKDSEELIY QKCRSTPYDD LLERSKTTIS
KLQFDHGALK SSEALYKKYI QKMDEEPSCP LCHHNMTSDE ACDLTSELTD EIQKLPDNIT
RAEKALKAEQ IKYENLLQLK PTILKVKELK DSLPQKKEEL KKVEELLGDS VSEYETLIAL
IGEPTHNMEL ANSMMGDMSL LDEALKDSAR LTKDLDLQKG QLPASYDSSV SMDDLQAEKS
KVSKELETER KELESAQNAV QQQMDALNRL REKKNSLKDR QIHLREGLQS LPQLKERLEK
LNSFLTTVAS EISELKAKIQ PLKLNLRAAI EEKERLKKSE SEKLAQLNSK YNSYKSTDHD
IQRLNKEAED YAKLDLRNEI KKLDEIIMAS KDKLRKLEAE ISLKTDELET IKTECSNQQT
VERDLKDNRE LKQLEDKEAK LRESCQVLDK QLGNLDFHSV SKEKVNLTKQ RDKATVRKGE
LLGQLGEIHS QVNKLQREID EPRFKESLKN FRKANYEIEV TRLCIEDLGQ YRLALEWALI
QFHSEKMEMI NRLIREYWRK IYRGNDIDYI QVKTDEVSSD ASADRRKTYN YRVVQSKNYS
EIEMRGRCSA GQRVLASLII RLALAETFSS NCGVLALDEP TTNLDRANIN SLCEALNCIV
EERQSQSNFM LIIITHDENF VSSLGKITSY HRVFRNEECK SVIRRVEAGP SKKALIDQ
