RAD54_DROME
ID RAD54_DROME Reviewed; 784 AA.
AC O76460; B6UXG7; B6UXH8; B6UXJ2; B6UXJ5; P91636; Q7K0T1; Q7KPH9;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=DNA repair and recombination protein RAD54-like {ECO:0000303|PubMed:9315669};
DE Short=DmRAD54 {ECO:0000303|PubMed:9315669};
DE EC=3.6.4.-;
DE AltName: Full=Protein okra {ECO:0000303|PubMed:9732269};
DE AltName: Full=RAD54 DNA repair protein {ECO:0000312|EMBL:AAC26857.1};
GN Name=okr {ECO:0000312|EMBL:AAF51168.1, ECO:0000312|FlyBase:FBgn0002989};
GN Synonyms=RAD54 {ECO:0000312|EMBL:CAA71278.1}; ORFNames=CG3736;
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] {ECO:0000305, ECO:0000312|EMBL:CAA71278.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=DP CN BW;
RX PubMed=9315669; DOI=10.1128/mcb.17.10.6097;
RA Kooistra R., Vreeken K., Zonneveld J.B., de Jong A., Eeken J.C.,
RA Osgood C.J., Buerstedde J.M., Lohman P.H., Pastink A.;
RT "The Drosophila melanogaster RAD54 homolog, DmRAD54, is involved in the
RT repair of radiation damage and recombination.";
RL Mol. Cell. Biol. 17:6097-6104(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC24577.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC TISSUE=Ovary {ECO:0000312|EMBL:AAC26857.1};
RX PubMed=9732269; DOI=10.1101/gad.12.17.2711;
RA Ghabrial A., Ray R.P., Schupbach T.;
RT "okra and spindle-B encode components of the RAD52 DNA repair pathway and
RT affect meiosis and patterning in Drosophila oogenesis.";
RL Genes Dev. 12:2711-2723(1998).
RN [3] {ECO:0000312|EMBL:AAF51168.1}
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAF51168.1}
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 [5] {ECO:0000312|EMBL:AAL39744.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39744.2}; TISSUE=Embryo;
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 (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305, ECO:0000312|EMBL:ACI97200.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 475-642.
RC STRAIN=MW11 {ECO:0000312|EMBL:ACI97200.1},
RC MW25 {ECO:0000312|EMBL:ACI97203.1}, MW27 {ECO:0000312|EMBL:ACI97204.1},
RC MW28 {ECO:0000312|EMBL:ACI97205.1}, MW38 {ECO:0000312|EMBL:ACI97221.1},
RC MW46 {ECO:0000312|EMBL:ACI97225.1}, MW56 {ECO:0000312|EMBL:ACI97226.1},
RC MW6 {ECO:0000312|EMBL:ACI97227.1}, MW63 {ECO:0000312|EMBL:ACI97228.1},
RC MW9 {ECO:0000312|EMBL:ACI97232.1}, NC301 {ECO:0000312|EMBL:ACI97206.1},
RC NC303 {ECO:0000312|EMBL:ACI97207.1}, NC304 {ECO:0000312|EMBL:ACI97208.1},
RC NC306 {ECO:0000312|EMBL:ACI97209.1}, NC307 {ECO:0000312|EMBL:ACI97210.1},
RC NC319 {ECO:0000312|EMBL:ACI97211.1}, NC322 {ECO:0000312|EMBL:ACI97212.1},
RC NC335 {ECO:0000312|EMBL:ACI97213.1}, NC336 {ECO:0000312|EMBL:ACI97214.1},
RC NC350 {ECO:0000312|EMBL:ACI97215.1}, NC357 {ECO:0000312|EMBL:ACI97216.1},
RC NC359 {ECO:0000312|EMBL:ACI97217.1}, NC361 {ECO:0000312|EMBL:ACI97218.1},
RC NC362 {ECO:0000312|EMBL:ACI97219.1}, NC375 {ECO:0000312|EMBL:ACI97220.1},
RC NC390 {ECO:0000312|EMBL:ACI97222.1}, NC397 {ECO:0000312|EMBL:ACI97223.1},
RC NC399 {ECO:0000312|EMBL:ACI97224.1}, NC732 {ECO:0000312|EMBL:ACI97229.1},
RC NC740 {ECO:0000312|EMBL:ACI97230.1}, and
RC NC774 {ECO:0000312|EMBL:ACI97231.1};
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 [7] {ECO:0000305}
RP FUNCTION, REGION, AND MUTAGENESIS OF 2-ARG--GLN-9 AND LYS-191.
RX PubMed=15105430; DOI=10.1074/jbc.m402648200;
RA Alexiadis V., Lusser A., Kadonaga J.T.;
RT "A conserved N-terminal motif in Rad54 is important for chromatin
RT remodeling and homologous strand pairing.";
RL J. Biol. Chem. 279:27824-27829(2004).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=17660539; DOI=10.1534/genetics.107.077693;
RA Wei D.S., Rong Y.S.;
RT "A genetic screen for DNA double-strand break repair mutations in
RT Drosophila.";
RL Genetics 177:63-77(2007).
RN [9] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-22, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:18327897};
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Involved in mitotic DNA repair and meiotic recombination.
CC Functions in the recombinational DNA repair pathway. Essential for
CC interhomolog gene conversion (GC), but may have a less important role
CC in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51
CC enhances the ATPase activity of okr/Rad54.
CC {ECO:0000269|PubMed:15105430, ECO:0000269|PubMed:17660539,
CC ECO:0000269|PubMed:9315669, ECO:0000269|PubMed:9732269}.
CC -!- SUBUNIT: Interacts (via N-terminus) with spn-A/Rad51. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9732269}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically at all
CC stages of fly development. {ECO:0000269|PubMed:9315669,
CC ECO:0000269|PubMed:9732269}.
CC -!- DISRUPTION PHENOTYPE: Eggs and embryos exhibit variable alterations
CC along the dorsal-ventral and anterior-posterior axes. There is a
CC reduction in the level of meiotic recombination and an increase in the
CC frequency of non-disjunction. Larvae have increased sensitivity to
CC ionizing radiation and MMS. {ECO:0000269|PubMed:9315669,
CC ECO:0000269|PubMed:9732269}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39744.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y10229; CAA71278.1; -; Genomic_DNA.
DR EMBL; AF069779; AAC24577.1; -; Genomic_DNA.
DR EMBL; AF069780; AAC26857.1; -; mRNA.
DR EMBL; AE014134; AAF51168.1; -; Genomic_DNA.
DR EMBL; AY069599; AAL39744.2; ALT_INIT; mRNA.
DR EMBL; FJ219215; ACI97200.1; -; Genomic_DNA.
DR EMBL; FJ219218; ACI97203.1; -; Genomic_DNA.
DR EMBL; FJ219219; ACI97204.1; -; Genomic_DNA.
DR EMBL; FJ219220; ACI97205.1; -; Genomic_DNA.
DR EMBL; FJ219221; ACI97206.1; -; Genomic_DNA.
DR EMBL; FJ219222; ACI97207.1; -; Genomic_DNA.
DR EMBL; FJ219223; ACI97208.1; -; Genomic_DNA.
DR EMBL; FJ219224; ACI97209.1; -; Genomic_DNA.
DR EMBL; FJ219225; ACI97210.1; -; Genomic_DNA.
DR EMBL; FJ219226; ACI97211.1; -; Genomic_DNA.
DR EMBL; FJ219227; ACI97212.1; -; Genomic_DNA.
DR EMBL; FJ219228; ACI97213.1; -; Genomic_DNA.
DR EMBL; FJ219229; ACI97214.1; -; Genomic_DNA.
DR EMBL; FJ219230; ACI97215.1; -; Genomic_DNA.
DR EMBL; FJ219231; ACI97216.1; -; Genomic_DNA.
DR EMBL; FJ219232; ACI97217.1; -; Genomic_DNA.
DR EMBL; FJ219233; ACI97218.1; -; Genomic_DNA.
DR EMBL; FJ219234; ACI97219.1; -; Genomic_DNA.
DR EMBL; FJ219235; ACI97220.1; -; Genomic_DNA.
DR EMBL; FJ219236; ACI97221.1; -; Genomic_DNA.
DR EMBL; FJ219237; ACI97222.1; -; Genomic_DNA.
DR EMBL; FJ219238; ACI97223.1; -; Genomic_DNA.
DR EMBL; FJ219239; ACI97224.1; -; Genomic_DNA.
DR EMBL; FJ219240; ACI97225.1; -; Genomic_DNA.
DR EMBL; FJ219241; ACI97226.1; -; Genomic_DNA.
DR EMBL; FJ219242; ACI97227.1; -; Genomic_DNA.
DR EMBL; FJ219243; ACI97228.1; -; Genomic_DNA.
DR EMBL; FJ219244; ACI97229.1; -; Genomic_DNA.
DR EMBL; FJ219245; ACI97230.1; -; Genomic_DNA.
DR EMBL; FJ219246; ACI97231.1; -; Genomic_DNA.
DR EMBL; FJ219247; ACI97232.1; -; Genomic_DNA.
DR RefSeq; NP_476661.1; NM_057313.5.
DR AlphaFoldDB; O76460; -.
DR SMR; O76460; -.
DR BioGRID; 59726; 28.
DR IntAct; O76460; 5.
DR STRING; 7227.FBpp0077357; -.
DR iPTMnet; O76460; -.
DR PaxDb; O76460; -.
DR DNASU; 33507; -.
DR EnsemblMetazoa; FBtr0077673; FBpp0077357; FBgn0002989.
DR GeneID; 33507; -.
DR KEGG; dme:Dmel_CG3736; -.
DR UCSC; CG3736-RA; d. melanogaster.
DR CTD; 33507; -.
DR FlyBase; FBgn0002989; okr.
DR VEuPathDB; VectorBase:FBgn0002989; -.
DR eggNOG; KOG0390; Eukaryota.
DR GeneTree; ENSGT00940000156897; -.
DR HOGENOM; CLU_000315_10_2_1; -.
DR InParanoid; O76460; -.
DR OMA; YTEHERM; -.
DR OrthoDB; 93727at2759; -.
DR PhylomeDB; O76460; -.
DR BioGRID-ORCS; 33507; 0 hits in 3 CRISPR screens.
DR ChiTaRS; okr; fly.
DR GenomeRNAi; 33507; -.
DR PRO; PR:O76460; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0002989; Expressed in mouthpart and 23 other tissues.
DR Genevisible; O76460; DM.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0043150; P:DNA synthesis involved in double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0046843; P:dorsal appendage formation; HMP:FlyBase.
DR GO; GO:0006302; P:double-strand break repair; IMP:FlyBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IMP:FlyBase.
DR GO; GO:0008298; P:intracellular mRNA localization; TAS:FlyBase.
DR GO; GO:0000711; P:meiotic DNA repair synthesis; IMP:UniProtKB.
DR GO; GO:0030716; P:oocyte fate determination; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IGI:FlyBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:FlyBase.
DR GO; GO:0006417; P:regulation of translation; TAS:FlyBase.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013967; Rad54_N.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08658; Rad54_N; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Meiosis; Mitosis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..784
FT /note="DNA repair and recombination protein RAD54-like"
FT /id="PRO_0000392522"
FT DOMAIN 172..346
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 503..660
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..9
FT /note="Required for chromatin remodeling, strand pairing
FT activities and coupling of ATPase activity"
FT /evidence="ECO:0000269|PubMed:15105430"
FT REGION 745..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 297..300
FT /note="DEGH box"
FT /evidence="ECO:0000255"
FT COMPBIAS 754..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 2..9
FT /note="Missing: Reduced ATPase activity and loss of
FT chromatin remodeling and strand pairing activities."
FT /evidence="ECO:0000269|PubMed:15105430"
FT MUTAGEN 191
FT /note="K->A: No ATPase or chromatin remodeling activity."
FT /evidence="ECO:0000269|PubMed:15105430"
FT MUTAGEN 191
FT /note="K->R: Partial ATPase and low chromatin remodeling
FT activity."
FT /evidence="ECO:0000269|PubMed:15105430"
FT CONFLICT 761
FT /note="K -> N (in Ref. 1; CAA71278 and 2; AAC26857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 784 AA; 89534 MW; B7B27FFF61C3AF63 CRC64;
MRRSLAPSQR GPLRPESRHS FTPPLLKKNK RSCQQELERE QELDRRRLGA LRDASNTSEL
PLPIRFTANS EYELAIAKVL ARKFKVPMDN YVPDYGGKRV LGVRRCISRR PLHDPMACNA
LVLFHPPAYT EHERMGMDPT KVLVHVVVDP LLSNILRPHQ REGVRFMYEC VEGKRGNFNG
CIMADEMGLG KTLQCVTLVW TLLRQGPECK PTINKAIVVS PSSLVKNWEK EFTKWLHGRL
LCLPMEGGTK ENTIRALEQF SMTSARLGTP VLLISYETFR IYAEILCKYE VGMVICDEGH
RLKNSDNLTY QALMGLKTKR RVLLSGTPIQ NDLTEYYSLV NFVNPEMLGT AAVFKRNFES
AILRGQNTDS TEQERQRAIE KTQELIGLVD QCIIRRTNQI LTKYLPVKFE MVICAKLTAI
QLELYTNFLK SDQVRRSLAD CNEKASLTAL ADITTLKKIC SHPDLIYEKL TAREKGFENS
QNVLPSNYKP KDLNPELSGK FMLLDFMLAA IRAEGNDKVV LISNYTQTLD LFEQLARKRK
YGFVRLDGTM SIKKRSKVVD RFNDPESDSF LFMLSSKAGG CGLNLIGANR LFMFDPDWNP
ANDEQAMARV WRDGQKKPCY IYRLVASGSI EEKILQRQTH KKSLSSTIID NNESAEKHFT
RDDLKDLFTF DANILSDTHD KLKCKRCVQN IQMKPPPEDT DCTSHLSQWY HCSNNRGLPD
NILAQAWMDC KCVSFVFHHR SQAQEIVPSA EEEATDQPEE KPESRKRSST PASDDSADED
FRGF
