ID ATR_YEAST Reviewed; 2368 AA.
AC P38111; D6VQD2; Q02580;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 01-MAY-2013, entry version 124.
DE RecName: Full=Serine/threonine-protein kinase MEC1;
DE EC=2.7.11.1;
DE AltName: Full=ATR homolog;
DE AltName: Full=DNA-damage checkpoint kinase MEC1;
DE AltName: Full=Mitosis entry checkpoint protein 1;
GN Name=MEC1; Synonyms=ESR1, SAD3; OrderedLocusNames=YBR136W;
GN ORFNames=YBR1012;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX PubMed=8065923; DOI=10.1093/nar/22.15.3104;
RA Kato R., Ogawa H.;
RT "An essential gene, ESR1, is required for mitotic cell growth, DNA
RT repair and meiotic recombination in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 22:3104-3112(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7926756;
RA Weinert T.A., Kiser G.L., Hartwell L.H.;
RT "Mitotic checkpoint genes in budding yeast and the dependence of
RT mitosis on DNA replication and repair.";
RL Genes Dev. 8:652-665(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091856; DOI=10.1002/yea.320100002;
RA Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F.,
RA Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M.,
RA Herbert C.J.;
RT "The sequence of 29.7 kb from the right arm of chromosome II reveals
RT 13 complete open reading frames, of which ten correspond to new
RT genes.";
RL Yeast 10:S1-S11(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
RA Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
RA Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
RA Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
RA Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
RA Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
RA Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
RA Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
RA Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
RA Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
RA Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
RA van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
RA Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
RA Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=8553072; DOI=10.1126/science.271.5247.357;
RA Sanchez Y., Desany B.A., Jones W.J., Liu Q., Wang B., Elledge S.J.;
RT "Regulation of RAD53 by the ATM-like kinases MEC1 and TEL1 in yeast
RT cell cycle checkpoint pathways.";
RL Science 271:357-360(1996).
RN [7]
RP PHOSPHORYLATION OF RPA2.
RX PubMed=8986766; DOI=10.1073/pnas.93.26.15075;
RA Brush G.S., Morrow D.M., Hieter P., Kelly T.J.;
RT "The ATM homologue MEC1 is required for phosphorylation of replication
RT protein A in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:15075-15080(1996).
RN [8]
RP INTERACTION WITH LCD1.
RX PubMed=11060031; DOI=10.1093/emboj/19.21.5801;
RA Rouse J., Jackson S.P.;
RT "LCD1: an essential gene involved in checkpoint control and regulation
RT of the MEC1 signalling pathway in Saccharomyces cerevisiae.";
RL EMBO J. 19:5801-5812(2000).
RN [9]
RP PHOSPHORYLATION OF LCD1, AND INTERACTION WITH LCD1.
RX PubMed=10950868;
RA Paciotti V., Clerici M., Lucchini G., Longhese M.P.;
RT "The checkpoint protein Ddc2, functionally related to S. pombe Rad26,
RT interacts with Mec1 and is regulated by Mec1-dependent phosphorylation
RT in budding yeast.";
RL Genes Dev. 14:2046-2059(2000).
RN [10]
RP FUNCTION.
RX PubMed=11140636; DOI=10.1038/35050000;
RA Downs J.A., Lowndes N.F., Jackson S.P.;
RT "A role for Saccharomyces cerevisiae histone H2A in DNA repair.";
RL Nature 408:1001-1004(2000).
RN [11]
RP IDENTIFICATION AS A KINASE, FUNCTION, AND MUTAGENESIS OF ASP-2224 AND
RP ASN-2229.
RX PubMed=11095737; DOI=10.1073/pnas.250475697;
RA Mallory J.C., Petes T.D.;
RT "Protein kinase activity of Tel1p and Mec1p, two Saccharomyces
RT cerevisiae proteins related to the human ATM protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13749-13754(2000).
RN [12]
RP FUNCTION, INTERACTION WITH LCD1, PHOSPHORYLATION OF LCD1, AND
RP MUTAGENESIS OF VAL-225; SER-552; LEU-781; PHE-1179; ASN-1700; ASP-2224
RP AND ASP-2243.
RX PubMed=11359899; DOI=10.1128/MCB.21.12.3913-3925.2001;
RA Paciotti V., Clerici M., Scotti M., Lucchini G., Longhese M.P.;
RT "Characterization of mec1 kinase-deficient mutants and of new
RT hypomorphic mec1 alleles impairing subsets of the DNA damage response
RT pathway.";
RL Mol. Cell. Biol. 21:3913-3925(2001).
RN [13]
RP FUNCTION.
RX PubMed=12181334; DOI=10.1091/mbc.02-02-0012;
RA Enomoto S., Glowczewski L., Berman J.;
RT "MEC3, MEC1, and DDC2 are essential components of a telomere
RT checkpoint pathway required for cell cycle arrest during senescence in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 13:2626-2638(2002).
RN [14]
RP FUNCTION.
RX PubMed=12792653; DOI=10.1038/sj.embor.embor871;
RA Redon C., Pilch D.R., Rogakou E.P., Orr A.H., Lowndes N.F.,
RA Bonner W.M.;
RT "Yeast histone 2A serine 129 is essential for the efficient repair of
RT checkpoint-blind DNA damage.";
RL EMBO Rep. 4:678-684(2003).
RN [15]
RP FUNCTION.
RX PubMed=15369670; DOI=10.1016/j.cell.2004.08.015;
RA Lisby M., Barlow J.H., Burgess R.C., Rothstein R.;
RT "Choreography of the DNA damage response: spatiotemporal relationships
RT among checkpoint and repair proteins.";
RL Cell 118:699-713(2004).
RN [16]
RP FUNCTION.
RX PubMed=15458641; DOI=10.1016/j.cub.2004.09.047;
RA Shroff R., Arbel-Eden A., Pilch D.R., Ira G., Bonner W.M.,
RA Petrini J.H.J., Haber J.E., Lichten M.;
RT "Distribution and dynamics of chromatin modification induced by a
RT defined DNA double-strand break.";
RL Curr. Biol. 14:1703-1711(2004).
RN [17]
RP PHOSPHORYLATION OF RTT107.
RX PubMed=14988729; DOI=10.1038/sj.emboj.7600129;
RA Rouse J.;
RT "Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA
RT synthesis after DNA damage.";
RL EMBO J. 23:1188-1197(2004).
RN [18]
RP FUNCTION, AND PHOSPHORYLATION OF SLX4.
RX PubMed=15975089; DOI=10.1042/BJ20050768;
RA Flott S., Rouse J.;
RT "Slx4 becomes phosphorylated after DNA damage in a Mec1/Tel1-dependent
RT manner and is required for repair of DNA alkylation damage.";
RL Biochem. J. 391:325-333(2005).
RN [19]
RP FUNCTION OF THE MEC1-LCD1 COMPLEX, AND PHOSPHORYLATION OF LCD1 AND
RP RAD53.
RX PubMed=16365046; DOI=10.1074/jbc.M507508200;
RA Ma J.-L., Lee S.-J., Duong J.K., Stern D.F.;
RT "Activation of the checkpoint kinase Rad53 by the phosphatidyl
RT inositol kinase-like kinase Mec1.";
RL J. Biol. Chem. 281:3954-3963(2006).
RN [20]
RP FUNCTION, INTERACTION WITH LCD1; RFA1 AND RFA2, AND MUTAGENESIS OF
RP 2360-MET--ILE-2362 AND 2367-PHE-TRP-2368.
RX PubMed=16148046; DOI=10.1091/mbc.E05-05-0405;
RA Nakada D., Hirano Y., Tanaka Y., Sugimoto K.;
RT "Role of the C-terminus of Mec1 checkpoint kinase in its localization
RT to sites of DNA damage.";
RL Mol. Biol. Cell 16:5227-5235(2005).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS
RP SPECTROMETRY.
RX PubMed=17563356; DOI=10.1073/pnas.0701622104;
RA Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
RT "Proteome-wide identification of in vivo targets of DNA damage
RT checkpoint kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-38, AND MASS
RP SPECTROMETRY.
RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth
RT phosphoproteome analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Serine/threonine protein kinase which activates
CC checkpoint signaling upon genotoxic stresses such as ionizing
CC radiation (IR), ultraviolet light (UV), or DNA replication
CC stalling, thereby acting as a DNA damage sensor. Recognizes the
CC substrate consensus sequence [ST]-Q. Recruited in complex with
CC protein LCD1 by the single-strand-binding protein complex RPA to
CC DNA lesions in order to initiate the DNA repair by homologous
CC recombination, after the MRX-complex and TEL1 are displaced.
CC Phosphorylates LCD1 and RPA2, a subunit of RPA, involved in DNA
CC replication, repair and recombination. Phosphorylates RAD9, CHK1
CC and RAD53, which leads to the activation of the CHK1 and RAD53
CC kinases involved in DNA damage repair cascade. Phosphorylates
CC histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage,
CC also involved in the regulation of DNA damage response mechanism.
CC Phosphorylates also SLX4 and RTT107 which are proteins involved in
CC genome stability. Required for cell growth and meiotic
CC recombination.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- SUBUNIT: Interacts with LCD1, which is required for localization
CC MEC1 to the RPA complex. Interacts directly with the RPA subunits
CC RFA1 and RFA2.
CC -!- INTERACTION:
CC Q04377:LCD1; NbExp=7; IntAct=EBI-6668, EBI-35652;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Localizes to nuclear DNA
CC repair foci in response to DNA double strand breaks. The
CC recruitment to DNA lesion sites requires its interaction with LCD1
CC and the presence of the RPA complex on DNA.
CC -!- DEVELOPMENTAL STAGE: Induced during meiosis.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC -!- SIMILARITY: Contains 1 FAT domain.
CC -!- SIMILARITY: Contains 1 FATC domain.
CC -!- SIMILARITY: Contains 5 HEAT repeats.
CC -!- SIMILARITY: Contains 1 PI3K/PI4K domain.
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DR EMBL; X75891; CAA53494.1; -; Genomic_DNA.
DR EMBL; U31109; AAA74482.1; -; Genomic_DNA.
DR EMBL; D11088; BAA01860.1; -; Genomic_DNA.
DR EMBL; Z36005; CAA85094.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07252.1; -; Genomic_DNA.
DR PIR; S46005; S46005.
DR RefSeq; NP_009694.3; NM_001178484.3.
DR ProteinModelPortal; P38111; -.
DR SMR; P38111; 2039-2307.
DR DIP; DIP-799N; -.
DR IntAct; P38111; 18.
DR MINT; MINT-659495; -.
DR STRING; 4932.YBR136W; -.
DR PaxDb; P38111; -.
DR PeptideAtlas; P38111; -.
DR EnsemblFungi; YBR136W; YBR136W; YBR136W.
DR GeneID; 852433; -.
DR KEGG; sce:YBR136W; -.
DR KEGG; sce:YBR140C; -.
DR CYGD; YBR136w; -.
DR SGD; S000000340; MEC1.
DR eggNOG; COG5032; -.
DR GeneTree; ENSGT00690000102233; -.
DR HOGENOM; HOG000034220; -.
DR KO; K02543; -.
DR OMA; HCENILL; -.
DR OrthoDB; EOG4TJ024; -.
DR NextBio; 971318; -.
DR Genevestigator; P38111; -.
DR GermOnline; YBR136W; Saccharomyces cerevisiae.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IC:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint; TAS:SGD.
DR GO; GO:0006975; P:DNA damage induced protein phosphorylation; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IMP:SGD.
DR GO; GO:0016572; P:histone phosphorylation; IMP:SGD.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
DR Gene3D; 1.10.1070.11; -; 2.
DR Gene3D; 1.25.10.10; -; 4.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR027011; Mec1.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR011990; TPR-like_helical.
DR InterPro; IPR012993; UME.
DR PANTHER; PTHR11139:SF5; PTHR11139:SF5; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF08064; UME; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00802; UME; 1.
DR SUPFAM; SSF48371; ARM-type_fold; 1.
DR SUPFAM; SSF56112; Kinase_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.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Complete proteome; DNA damage;
KW DNA repair; Kinase; Meiosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1 2368 Serine/threonine-protein kinase MEC1.
FT /FTId=PRO_0000088836.
FT DOMAIN 1399 1944 FAT.
FT DOMAIN 2082 2368 PI3K/PI4K.
FT DOMAIN 2336 2368 FATC.
FT REGION 2140 2368 Binding to the RPA complex.
FT MOD_RES 37 37 Phosphoserine.
FT MOD_RES 38 38 Phosphoserine; by ATM or ATR.
FT MUTAGEN 225 225 V->G: In MEC1-101; impairs both the G1/S
FT and intra-S damage checkpoints but not
FT the G2/M damage checkpoint; when
FT associated with P-552 and S-781.
FT MUTAGEN 552 552 S->P: In MEC1-101; impairs both the G1/S
FT and intra-S damage checkpoints but not
FT the G2/M damage checkpoint; when
FT associated with S-225 and S-781.
FT MUTAGEN 781 781 L->S: In MEC1-101; impairs both the G1/S
FT and intra-S damage checkpoints but not
FT the G2/M damage checkpoint; when
FT associated with S-225 and P-552.
FT MUTAGEN 1179 1179 F->S: In MEC1-100; impairs both the G1/S
FT and intra-S damage checkpoints but not
FT the G2/M damage checkpoint; when
FT associated with S-1700.
FT MUTAGEN 1700 1700 N->S: In MEC1-100; impairs both the G1/S
FT and intra-S damage checkpoints but not
FT the G2/M damage checkpoint; when
FT associated with S-1179.
FT MUTAGEN 2224 2224 D->A: Impairs kinase activity; when
FT associated with K-2229.
FT MUTAGEN 2229 2229 N->K: Impairs kinase activity; when
FT associated with A-2224.
FT MUTAGEN 2243 2243 D->E: Impairs kinase activity.
FT MUTAGEN 2360 2362 MYI->AAA: In MEC1-85; disrupts
FT interaction with RFA1 and severely
FT impairs kinase activity.
FT MUTAGEN 2367 2368 FW->AA: In MEC1-87; decreases the level
FT of MEC1 and impairs viability.
FT CONFLICT 197 197 N -> D (in Ref. 1; BAA01860).
FT CONFLICT 716 716 S -> P (in Ref. 2; AAA74482).
FT CONFLICT 1255 1255 K -> Q (in Ref. 2; AAA74482).
FT CONFLICT 1276 1276 L -> G (in Ref. 2; AAA74482).
SQ SEQUENCE 2368 AA; 273342 MW; C06AEF9F0484A615 CRC64;
MESHVKYLDE LILAIKDLNS GVDSKVQIKK VPTDPSSSQE YAKSLKILNT LIRNLKDQRR
NNIMKNDTIF SKTVSALALL LEYNPFLLVM KDSNGNFEIQ RLIDDFLNIS VLNYDNYHRI
WFMRRKLGSW CKACVEFYGK PAKFQLTAHF ENTMNLYEQA LTEVLLGKTE LLKFYDTLKG
LYILLYWFTS EYSTFGNSIA FLDSSLGFTK FDFNFQRLIR IVLYVFDSCE LAALEYAEIQ
LKYISLVVDY VCNRTISTAL DAPALVCCEQ LKFVLTTMHH FLDNKYGLLD NDPTMAKGIL
RLYSLCISND FSKCFVDHFP IDQWADFSQS EHFPFTQLTN KALSIVYFDL KRRSLPVEAL
KYDNKFNIWV YQSEPDSSLK NVTSPFDDRY KQLEKLRLLV LKKFNKTERG TLLKYRVNQL
SPGFFQRAGN DFKLILNEAS VSIQTCFKTN NITRLTSWTV ILGRLACLES EKFSGTLPNS
TKDMDNWYVC HLCDIEKTGN PFVRINPNRP EAAGKSEIFR ILHSNFLSHP NIDEFSESLL
SGILFSLHRI FSHFQPPKLT DGNGQINKSF KLVQKCFMNS NRYLRLLSTR IIPLFNISDS
HNSEDEHTAT LIKFLQSQKL PVVKENLVIA WTQLTLTTSN DVFDTLLLKL IDIFNSDDYS
LRIMMTLQIK NMAKILKKTP YQLLSPILPV LLRQLGKNLV ERKVGFQNLI ELLGYSSKTI
LDIFQRYIIP YAIIQYKSDV LSEIAKIMCD GDTSLINQMK VNLLKKNSRQ IFAVALVKHG
LFSLDILETL FLNRAPTFDK GYITAYLPDY KTLAEITKLY KNSVTKDASD SENANMILCS
LRFLITNFEK DKRHGSKYKN INNWTDDQEQ AFQKKLQDNI LGIFQVFSSD IHDVEGRTTY
YEKLRVINGI SFLIIYAPKK SIISALAQIS ICLQTGLGLK EVRYEAFRCW HLLVRHLNDE
ELSTVIDSLI AFILQKWSEF NGKLRNIVYS ILDTLIKEKS DLILKLKPYT TLALVGKPEL
GILARDGQFA RMVNKIRSTT DLIPIFANNL KSSNKYVINQ NLDDIEVYLR RKQTERSIDF
TPKKVGQTSD ITLVLGALLD TSHKFRNLDK DLCEKCAKCI SMIGVLDVTK HEFKRTTYSE
NEVYDLNDSV QTIKFLIWVI NDILVPAFWQ SENPSKQLFV ALVIQESLKY CGLSSESWDM
NHKELYPNEA KLWEKFNSVS KTTIYPLLSS LYLAQSWKEY VPLKYPSNNF KEGYKIWVKR
FTLDLLKTGT TENHPLHVFS SLIREDDGSL SNFLLPYISL DIIIKAEKGT PYADILNGII
IEFDSIFTCN LEGMNNLQVD SLRMCYESIF RVFEYCKKWA TEFKQNYSKL HGTFIIKDTK
TTNMLLRIDE FLRTTPSDLL AQRSLETDSF ERSALYLEQC YRQNPHDKNQ NGQLLKNLQI
TYEEIGDIDS LDGVLRTFAT GNLVSKIEEL QYSENWKLAQ DCFNVLGKFS DDPKTTTRML
KSMYDHQLYS QIISNSSFHS SDGKISLSPD VKEWYSIGLE AANLEGNVQT LKNWVEQIES
LRNIDDREVL LQYNIAKALI AISNEDPLRT QKYIHNSFRL IGTNFITSSK ETTLLKKQNL
LMKLHSLYDL SFLSSAKDKF EYKSNTTILD YRMERIGADF VPNHYILSMR KSFDQLKMNE
QADADLGKTF FTLAQLARNN ARLDIASESL MHCLERRLPQ AELEFAEILW KQGENDRALK
IVQEIHEKYQ ENSSVNARDR AAVLLKFTEW LDLSNNSASE QIIKQYQDIF QIDSKWDKPY
YSIGLYYSRL LERKKAEGYI TNGRFEYRAI SYFLLAFEKN TAKVRENLPK VITFWLDIAA
ASISEAPGNR KEMLSKATED ICSHVEEALQ HCPTYIWYFV LTQLLSRLLH SHQSSAQIIM
HILLSLAVEY PSHILWYITA LVNSNSSKRV LRGKHILEKY RQHSQNPHDL VSSALDLTKA
LTRVCLQDVK SITSRSGKSL EKDFKFDMNV APSAMVVPVR KNLDIISPLE SNSMRGYQPF
RPVVSIIRFG SSYKVFSSLK KPKQLNIIGS DGNIYGIMCK KEDVRQDNQY MQFATTMDFL
LSKDIASRKR SLGINIYSVL SLREDCGILE MVPNVVTLRS ILSTKYESLK IKYSLKSLHD
RWQHTAVDGK LEFYMEQVDK FPPILYQWFL ENFPDPINWF NARNTYARSY AVMAMVGHIL
GLGDRHCENI LLDIQTGKVL HVDFDCLFEK GKRLPVPEIV PFRLTPNLLD ALGIIGTEGT
FKKSSEVTLA LMRKNEVALM NVIETIMYDR NMDHSIQKAL KVLRNKIRGI DPQDGLVLSV
AGQTETLIQE ATSEDNLSKM YIGWLPFW
//
