ID M9PFS0_DROME Unreviewed; 2471 AA.
AC M9PFS0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=mTor {ECO:0000313|EMBL:AGB92962.1,
GN ECO:0000313|FlyBase:FBgn0021796};
GN Synonyms=5092 {ECO:0000313|EMBL:AGB92962.1}, CT16317
GN {ECO:0000313|EMBL:AGB92962.1}, CT24745 {ECO:0000313|EMBL:AGB92962.1},
GN CT24817 {ECO:0000313|EMBL:AGB92962.1}, Dmel\CG5092
GN {ECO:0000313|EMBL:AGB92962.1}, DmTOR {ECO:0000313|EMBL:AGB92962.1},
GN dTOR {ECO:0000313|EMBL:AGB92962.1}, dTor
GN {ECO:0000313|EMBL:AGB92962.1}, dtor {ECO:0000313|EMBL:AGB92962.1},
GN dTORC1 {ECO:0000313|EMBL:AGB92962.1}, FRAP/TOR
GN {ECO:0000313|EMBL:AGB92962.1}, l(2)k17004
GN {ECO:0000313|EMBL:AGB92962.1}, Mtor {ECO:0000313|EMBL:AGB92962.1},
GN mTOR {ECO:0000313|EMBL:AGB92962.1}, TOR {ECO:0000313|EMBL:AGB92962.1},
GN Tor {ECO:0000313|EMBL:AGB92962.1}, tor {ECO:0000313|EMBL:AGB92962.1},
GN TOR-C1 {ECO:0000313|EMBL:AGB92962.1}, Tor-C1
GN {ECO:0000313|EMBL:AGB92962.1}, TORC1 {ECO:0000313|EMBL:AGB92962.1},
GN Torc1 {ECO:0000313|EMBL:AGB92962.1};
GN ORFNames=CG5092 {ECO:0000313|EMBL:AGB92962.1,
GN ECO:0000313|FlyBase:FBgn0021796}, Dmel_CG5092
GN {ECO:0000313|EMBL:AGB92962.1};
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:AGB92962.1, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AGB92962.1, 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|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|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|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:AGB92962.1, 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:AGB92962.1, 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:AGB92962.1, 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:AGB92962.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031}.
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DR EMBL; AE014134; AGB92962.1; -; Genomic_DNA.
DR RefSeq; NP_001260427.1; NM_001273498.1.
DR SMR; M9PFS0; -.
DR EnsemblMetazoa; FBtr0336615; FBpp0307598; FBgn0021796.
DR GeneID; 47396; -.
DR AGR; FB:FBgn0021796; -.
DR FlyBase; FBgn0021796; mTor.
DR VEuPathDB; VectorBase:FBgn0021796; -.
DR GeneTree; ENSGT00930000151037; -.
DR OMA; MRQHSAK; -.
DR OrthoDB; 8448at2759; -.
DR BioGRID-ORCS; 47396; 2 hits in 3 CRISPR screens.
DR ChiTaRS; Egfr; fly.
DR GenomeRNAi; 47396; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0021796; Expressed in eye disc (Drosophila) and 25 other cell types or tissues.
DR ExpressionAtlas; M9PFS0; baseline and differential.
DR GO; GO:0031931; C:TORC1 complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IEA:UniProt.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024585; mTOR_dom.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR_cat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS50005; TPR; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|PeptideAtlas:M9PFS0};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1350..1904
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT REPEAT 1408..1441
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 2078..2390
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2439..2471
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2365..2390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2471 AA; 281162 MW; 2F07B7F9290BDB95 CRC64;
MSTTSVVQQF VNGLKSRNRN VQNKATQDLL FYVKTELREM SQEELAQFFD EFDHHIFTMV
NATDINEKKG GALAMKCLIN CEGSLTARKG ISPYLNRLRD LLLINDVSVM EIAARSLVKL
ANMPTSKGAD SFDFDIKKAF EVLRGERQEY RRHSAVFILR ELAIALPTYF YQHILTFFEV
IFNAIFDPKP AIRESAGEAL RAALIVTAQR ESTKQSSEPQ WYRICYDEAN GSFNADLGSS
KDQKGVTRDD RIHGGLVVFN ELFRCANATW ERRYTSLKTL FPKTQHNKFL EASSSSSMGS
QLNTLVPRLK VPFIDKLGST QTHLGEGEHH KGVAKFASQH NVLESAYAQE ILQEHYTSIC
DNVLEQRTSK SPYVQQALLQ ILPRLAAFNR AVFVEKYLQT CVSHLMQILR GKEKDRTVAY
ITIGYMAVAV QSAIEVHLSS IMTSVKVALP SKDLTSKRKV PVDPAVFACI TLLAHAVKSE
IADDVKDILE QMFYTGLSPA LTVCLRELSE NVPQLKSAIT EGLIGILSQV LMNKAAILPY
TALPTIAIDG SLMQNGDGAT TVLALKTLGT FNFEEQNMLD FVQRCADYFI VHEQQEIRLE
AVQTCTRLLK LAVQSSESME NSKTLSDTVS HVIERLLMVA ITDMDCNVRI RILRSLDETF
DGKLAQPESL NSLFITLHDE IFEIRELAMV TIGRLSSINP AYVMPKLRTT MIELITDLKY
SGMSRNKEQS AKMLDHLVIS TPRLISSYMN PILKALVPKL HEPESNPGVI LNVLRTIGDL
AEVNGGSDEM ELWADDLLSI LLEMLGDAGS PDKRGVALWT LGQLISATGR VVTPYHKYPV
LIDILINFLK TEQRRSIRRE TIRVLGLLGA MDPYKHKMNK GLIDSQKDNV LIAYSDGKVD
ESQDISTAEL LVNMGNALDE YYPAVAIAAL MRILRDPTLS TRHTSVVQAV TFIFQSLGIK
CVPYLAQVLP NLLDNVRTAD NNLREFLFQQ LAILVAFVKL HIISYMGDIF KLIKEFWTIN
TPLQNTLINL IEQIAVALGC EFRDYLAELI PQILRVLQHD NSKDRMVTRR LLQALQKFGS
TLGYYLPLIL PPIVKLFDSP YVPQQVSMVA LETINNLACQ LDFTDFSSRI IHPLVRVLDA
EPELRDQAMT TLRSLAKQLG KKYLVFVPMV QRTLNKHRIV DPEYEELLSK IKSCSTLADS
YGAGESELRP SRFKNNEPFV TDRNSNNKNL QVTTNELRTA WQVTRRVSKD DWVEWLKRLS
IGLLKESPSH ALRACRSLAQ EYDTLLRDLF NAAFISCWTE LSPDLKNELT QSLIQALQVT
DMPEITQTIL NLAEFMEHCD RDPIPIETKL LGTRAMACRA YAKALRYKEE EFLLREDSQV
FESLILINNK LQQREAAEGL LTRYRNAANE LNVQGRWYEK LHNWDEALEH YERNLKTDSS
DLEARLGHMR CLEALGDWSE LSNVTKHEWE NFGTEAKSRA GPLAAVAAWG LQDWEAMREY
VRCIPEDTQD GSYYRAVLAV HHDDFETAQR LIDETRDLLD TELTSMAGES YERAYGAMVC
VQMLAELEEV IQYKLIPERR EPLKTMWWKR LQGGQRLVED WRRIIQVHSL VVKPHEDIHT
WLKYASLCRK SGSLHLSHKT LVMLLGTDPK LNPNQPLPCN QPQVTYAYTK YMAANNQLQE
AYEQLTHFVS TYSQELSCLP PEALKQQDQR LMARCYLRMA TWQNKLQDSI RPDAIQGALE
CFEKATSYDP NWYKAWHLWA YMNFKVVQAQ KSALDKQQPP GASMGMTMGS GLDSDLMIIQ
RYAVPAVQGF FRSISLIKGN SLQDTLRLLT LWFDYGNHAE VYEALLSGMK LIEINTWLQV
IPQLIARIDT HRQLVGQLIH QLLMDIGKNH PQALVYPLTV ASKSASLARR NAAFKILDSM
RKHSPTLVEQ AVMCSEELIR VAILWHEQWH EGLEEASRLY FGDRNVKGMF EILEPLHAML
ERGPQTLKET SFSQAYGREL TEAYEWSQRY KTSAVVMDLD RAWDIYYHVF QKISRQLPQL
TSLELPYVSP KLMTCKDLEL AVPGSYNPGQ ELIRISIIKT NLQVITSKQR PRKLCIRGSN
GKDYMYLLKG HEDLRQDERV MQLFSLVNTL LLDDPDTFRR NLAIQRYAVI PLSTNSGLIG
WVPHCDTLHT LIRDYRDKKK VPLNQEHRTM LNFAPDYDHL TLMQKVEVFE HALGQTQGDD
LAKLLWLKSP SSELWFERRN NYTRSLAVMS MVGYILGLGD RHPSNLMLDR MSGKILHIDF
GDCFEVAMTR EKFPEKIPFR LTRMLIKAME VTGIEGTYRR TCESVMLVLR RNKDSLMAVL
EAFVYDPLLN WRLLDVDKKG NDAVAGAGAP GGRGGSGMQD SLSNSVEDSL PMAKSKPYDP
TLQQGGLHNN VADETNSKAS QVIKRVKCKL TGTDFQTEKS VNEQSQVELL IQQATNNENL
CQCYIGWCPF W
//
