ID M9NG38_DROME Unreviewed; 1527 AA.
AC M9NG38;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=MAGUK p55 subfamily member 5 {ECO:0000256|ARBA:ARBA00032294};
GN Name=sdt {ECO:0000313|EMBL:AFH07288.1,
GN ECO:0000313|FlyBase:FBgn0261873};
GN Synonyms=anon-EST:fe2E6 {ECO:0000313|EMBL:AFH07288.1}, BP1063
GN {ECO:0000313|EMBL:AFH07288.1}, CG12657 {ECO:0000313|EMBL:AFH07288.1},
GN CG12658 {ECO:0000313|EMBL:AFH07288.1}, CG15339
GN {ECO:0000313|EMBL:AFH07288.1}, CG15340 {ECO:0000313|EMBL:AFH07288.1},
GN CG15341 {ECO:0000313|EMBL:AFH07288.1}, CG15342
GN {ECO:0000313|EMBL:AFH07288.1}, CG1617 {ECO:0000313|EMBL:AFH07288.1},
GN cGUK1 {ECO:0000313|EMBL:AFH07288.1}, cMAGUK1
GN {ECO:0000313|EMBL:AFH07288.1}, Dmel\CG32717
GN {ECO:0000313|EMBL:AFH07288.1}, l(1)7Ef {ECO:0000313|EMBL:AFH07288.1},
GN pal1 {ECO:0000313|EMBL:AFH07288.1}, PALS1
GN {ECO:0000313|EMBL:AFH07288.1}, Pals1 {ECO:0000313|EMBL:AFH07288.1},
GN SDT {ECO:0000313|EMBL:AFH07288.1}, Sdt {ECO:0000313|EMBL:AFH07288.1},
GN Std {ECO:0000313|EMBL:AFH07288.1}, std {ECO:0000313|EMBL:AFH07288.1};
GN ORFNames=CG32717 {ECO:0000313|EMBL:AFH07288.1,
GN ECO:0000313|FlyBase:FBgn0261873}, Dmel_CG32717
GN {ECO:0000313|EMBL:AFH07288.1};
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:0000313|EMBL:AFH07288.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AFH07288.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., 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., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|EMBL:AFH07288.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|EMBL:AFH07288.1, ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|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 [4] {ECO:0000313|EMBL:AFH07288.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AFH07288.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AFH07288.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AFH07288.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AFH07288.1, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004236}. Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004184}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR EMBL; AE014298; AFH07288.1; -; Genomic_DNA.
DR RefSeq; NP_001245574.1; NM_001258645.1.
DR SMR; M9NG38; -.
DR DNASU; 44861; -.
DR EnsemblMetazoa; FBtr0308218; FBpp0300538; FBgn0261873.
DR GeneID; 44861; -.
DR AGR; FB:FBgn0261873; -.
DR CTD; 44861; -.
DR FlyBase; FBgn0261873; sdt.
DR VEuPathDB; VectorBase:FBgn0261873; -.
DR GeneTree; ENSGT00940000156087; -.
DR OrthoDB; 2873706at2759; -.
DR BioGRID-ORCS; 44861; 0 hits in 1 CRISPR screen.
DR ChiTaRS; sdt; fly.
DR GenomeRNAi; 44861; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0261873; Expressed in spermathecum and 33 other cell types or tissues.
DR ExpressionAtlas; M9NG38; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005918; C:septate junction; TAS:FlyBase.
DR GO; GO:0035003; C:subapical complex; IPI:FlyBase.
DR GO; GO:0004385; F:guanylate kinase activity; ISS:FlyBase.
DR GO; GO:0045176; P:apical protein localization; IMP:FlyBase.
DR GO; GO:0007043; P:cell-cell junction assembly; NAS:FlyBase.
DR GO; GO:0040003; P:chitin-based cuticle development; IMP:FlyBase.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:FlyBase.
DR GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:FlyBase.
DR GO; GO:0048699; P:generation of neurons; IBA:GO_Central.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; TAS:FlyBase.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IBA:GO_Central.
DR GO; GO:0002009; P:morphogenesis of an epithelium; NAS:FlyBase.
DR GO; GO:0042461; P:photoreceptor cell development; IMP:FlyBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0045186; P:zonula adherens assembly; IMP:FlyBase.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 2.
DR CDD; cd12036; SH3_MPP5; 1.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR035601; MPP5_SH3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR PANTHER; PTHR23122:SF14; PROTEIN PALS1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 1.
DR Pfam; PF00595; PDZ; 2.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9NG38};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000313|EMBL:AFH07288.1}.
FT DOMAIN 54..103
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 903..959
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 1052..1131
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1157..1228
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1307..1506
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1527 AA; 165388 MW; 09F321ED607276CC CRC64;
MQANSSRSNL SAQSSGTPSA STISSSQGKQ QVVELSGYVI ILVENVEGKI KLYGSPPDRD
NLEVGDEILE VNGLTLENIS RTEVIRHIHD CIKSCTICLR VRKKNDSRLA WDIGNSVQDA
FVIAVEEHAR ERLQRLAALN RVTPVDITQL SKKLLEDVIV HQASDVHSYS TSASAAAIAS
SSNRSQQQQQ QQQQHQLLSA AYELQQQQQL QLQQQQQQQN SPTSSISIGR TELLLGDQSL
RQDPRGNRRR SGSSIVVLDG DDLKPCLPDD YISGQHHLNH QQQLQLQQQL QQQHPLQQQH
YRTHSGDIRE IDQEMLTMLS VNQDNGPHRE MAVDCPDTFI ARNKTPPRYP PPRPPQKQHQ
ATTAMAATQV AQQQTPSHKL QATLSSDPNG NSNSNNNSHI VGISSSSSSN NSSITDDFLC
VVDGLYQGRK DTASPSSSAF DEVMSKHTLD SFGSIAYRHL HQQHQATSNG NSSSNTSNTN
SNTNSNTNSN SNTNGNTSNN TAVSTKTATV TKTGVSSSNS NSNSLNSSNS SMHTSSSSSG
HSSNIASATS SSSATSSSTV PDDLSLAPPG YEVSQQQQQQ HLVATPVTML LPPMAKHREL
PVDVPDSFIE MVKTTPRYPP PAHLSSRGSL LSNGSASTAH TTLSSMGVAP SPVTATAAAA
ASASAACATT AVAAAAVSGV ADGDARRVAD ELNGNAKPVP PPRDHLRVEK DGRLVNCSPA
PQLPDRRAPG NASSGSSGAT THPLQHQQIA QIVEPTLEQL DSIKKYQEQL RRRREEEERI
AQQNEFLRNS LRGSRKLKAL QDTATPGKAV AQQQQQATLA TQVVGVENEA YLPDEDQPQA
EQIDGYGELI AALTRLQNQL SKSGLSTLAG RVSAAHSVLA SASVAHVLAA RTAVLQRRRS
RVSGPLHHSS LGLQKDIVEL LTQSNTAAAI ELGNLLTSHE MEGLLLAHDR IANHTDGTPS
PTPTPTPAIG AATGSTLSSP VAGPKRNLGM VVPPPVVPPP LAQRGAMPLP RGESPPPVPM
PPLATMPMSM PVNLPMSACF GTLNDQNDNI RIIQIEKSTE PLGATVRNEG EAVVIGRIVR
GGAAEKSGLL HEGDEILEVN GQELRGKTVN EVCALLGAMQ GTLTFLIVPA GSPPSVGVMG
GTTGSQLAGL GGAHRDTAVL HVRAHFDYDP EDDLYIPCRE LGISFQKGDV LHVISREDPN
WWQAYREGEE DQTLAGLIPS QSFQHQRETM KLAIAEEAGL ARSRGKDGSG SKGATLLCAR
KGRKKKKKAS SEAGYPLYAT TAPDETDPEE ILTYEEVALY YPRATHKRPI VLIGPPNIGR
HELRQRLMAD SERFSAAVPL FYLLEERLKP AKIKAQVKDT SRARREGEVP GVDYHFITRQ
AFEADILARR FVEHGEYEKA YYGTSLEAIR TVVASGKICV LNLHPQSLKL LRASDLKPYV
VLVAPPSLDK LRQKKLRNGE PFKEEELKDI IATARDMEAR WGHLFDMIII NNDTERAYHQ
LLAEINSLER EPQWVPAQWV HNNRDES
//