ATM_YEAST
ID ATM_YEAST Reviewed; 2787 AA.
AC P38110; D6VPR6;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Serine/threonine-protein kinase TEL1;
DE EC=2.7.11.1;
DE AltName: Full=ATM homolog;
DE AltName: Full=DNA-damage checkpoint kinase TEL1;
DE AltName: Full=Telomere length regulation protein 1;
GN Name=TEL1; OrderedLocusNames=YBL088C; ORFNames=YBL0706;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
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., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 1412.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1284, FUNCTION, AND MUTAGENESIS OF
RP 2611-GLY-ASP-2612; ASN-2616 AND ASP-2631.
RX PubMed=7671310; DOI=10.1016/0092-8674(95)90479-4;
RA Greenwell P.W., Kronmal S.L., Porter S.E., Gassenhuber J., Obermaier B.,
RA Petes T.D.;
RT "TEL1, a gene involved in controlling telomere length in S. cerevisiae, is
RT homologous to the human ataxia telangiectasia gene.";
RL Cell 82:823-829(1995).
RN [5]
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 cell
RT cycle checkpoint pathways.";
RL Science 271:357-360(1996).
RN [6]
RP IDENTIFICATION AS A KINASE, FUNCTION, AND MUTAGENESIS OF 2611-GLY-ASP-2612;
RP ASN-2616 AND ASP-2631.
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 cerevisiae
RT proteins related to the human ATM protein kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13749-13754(2000).
RN [7]
RP FUNCTION.
RX PubMed=11707419; DOI=10.1093/emboj/20.22.6485;
RA Clerici M., Paciotti V., Baldo V., Romano M., Lucchini G., Longhese M.P.;
RT "Hyperactivation of the yeast DNA damage checkpoint by TEL1 and DDC2
RT overexpression.";
RL EMBO J. 20:6485-6498(2001).
RN [8]
RP FUNCTION.
RX PubMed=11239397; DOI=10.1016/s0092-8674(01)00227-6;
RA Myung K., Datta A., Kolodner R.D.;
RT "Suppression of spontaneous chromosomal rearrangements by S phase
RT checkpoint functions in Saccharomyces cerevisiae.";
RL Cell 104:397-408(2001).
RN [9]
RP FUNCTION.
RX PubMed=11544181; DOI=10.1101/gad.208701;
RA D'Amours D., Jackson S.P.;
RT "The yeast Xrs2 complex functions in S phase checkpoint regulation.";
RL Genes Dev. 15:2238-2249(2001).
RN [10]
RP FUNCTION.
RX PubMed=11430828; DOI=10.1016/s1097-2765(01)00270-2;
RA Usui T., Ogawa H., Petrini J.H.J.;
RT "A DNA damage response pathway controlled by Tel1 and the Mre11 complex.";
RL Mol. Cell 7:1255-1266(2001).
RN [11]
RP RECRUITMENT TO DNA LESIONS.
RX PubMed=11983176; DOI=10.1016/s1097-2765(02)00507-5;
RA Rouse J., Jackson S.P.;
RT "Lcd1p recruits Mec1p to DNA lesions in vitro and in vivo.";
RL Mol. Cell 9:857-869(2002).
RN [12]
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., 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 [13]
RP FUNCTION, INTERACTION WITH XRS2, AND ASSOCIATION WITH DNA DOUBLE-STRAND
RP BREAKS.
RX PubMed=12923051; DOI=10.1101/gad.1099003;
RA Nakada D., Matsumoto K., Sugimoto K.;
RT "ATM-related Tel1 associates with double-strand breaks through an Xrs2-
RT dependent mechanism.";
RL Genes Dev. 17:1957-1962(2003).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [15]
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., Petrini J.H.J.,
RA Haber J.E., Lichten M.;
RT "Distribution and dynamics of chromatin modification induced by a defined
RT DNA double-strand break.";
RL Curr. Biol. 14:1703-1711(2004).
RN [16]
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 [17]
RP FUNCTION, AND MUTAGENESIS OF GLU-1319.
RX PubMed=16228207; DOI=10.1007/s00294-005-0020-7;
RA Chakhparonian M., Faucher D., Wellinger R.J.;
RT "A mutation in yeast Tel1p that causes differential effects on the DNA
RT damage checkpoint and telomere maintenance.";
RL Curr. Genet. 48:310-322(2005).
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling upon genotoxic stresses such as ionizing radiation (IR),
CC ultraviolet light (UV), or DNA replication stalling, thereby acting as
CC a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-
CC Q. Recruited by the MRX-complex to sites of DNA lesions immediately
CC after damage to initiate non-homologous end-joining (NHEJ).
CC Subsequently displaced by the RPA complex in a reaction probably
CC involving the SAE2 protein. Phosphorylates MRE11 and XRS2, 2 subunits
CC of the MRX-complex. The phosphorylation of MRE11 is a feedback response
CC from the checkpoint signaling pathway. Phosphorylates RAD9, CHK1 and
CC RAD53, leading to the activation of the CHK1 and RAD23 kinases involved
CC in the DNA damage response cascade. Phosphorylates histone H2A to form
CC H2AS128ph (gamma-H2A) at sites of DNA damage, also involved in the
CC regulation of DNA damage response mechanism. Phosphorylates also SLX4
CC and RTT107 which are involved in genome stability. Required for the
CC control of telomere length and genome stability.
CC {ECO:0000269|PubMed:11095737, ECO:0000269|PubMed:11239397,
CC ECO:0000269|PubMed:11430828, ECO:0000269|PubMed:11544181,
CC ECO:0000269|PubMed:11707419, ECO:0000269|PubMed:12792653,
CC ECO:0000269|PubMed:12923051, ECO:0000269|PubMed:15369670,
CC ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15975089,
CC ECO:0000269|PubMed:16228207, ECO:0000269|PubMed:7671310,
CC ECO:0000269|PubMed:8553072}.
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 -!- 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;
CC -!- SUBUNIT: Interacts with XRS2 and associates with DNA double-strand
CC breaks. {ECO:0000269|PubMed:12923051}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15369670}.
CC Chromosome, telomere {ECO:0000269|PubMed:15369670}. Note=Localizes to
CC nuclear DNA repair foci in response to DNA double strand breaks.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000305}.
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DR EMBL; X79489; CAA56016.1; -; Genomic_DNA.
DR EMBL; Z35849; CAA84909.1; -; Genomic_DNA.
DR EMBL; U31331; AAA69802.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07036.2; -; Genomic_DNA.
DR PIR; S45416; S45416.
DR RefSeq; NP_009465.2; NM_001178328.2.
DR PDB; 3H7B; X-ray; 1.88 A; C/F=549-557.
DR PDB; 3H9H; X-ray; 2.00 A; C/F=549-557.
DR PDB; 3H9S; X-ray; 2.70 A; C=549-557.
DR PDB; 6JXA; EM; 4.30 A; A=1-2787.
DR PDB; 6JXC; EM; 4.10 A; A=1-2787.
DR PDB; 6S8F; EM; 4.00 A; F/H=968-2787.
DR PDBsum; 3H7B; -.
DR PDBsum; 3H9H; -.
DR PDBsum; 3H9S; -.
DR PDBsum; 6JXA; -.
DR PDBsum; 6JXC; -.
DR PDBsum; 6S8F; -.
DR SMR; P38110; -.
DR BioGRID; 32616; 189.
DR DIP; DIP-6524N; -.
DR IntAct; P38110; 6.
DR MINT; P38110; -.
DR STRING; 4932.YBL088C; -.
DR iPTMnet; P38110; -.
DR MaxQB; P38110; -.
DR PaxDb; P38110; -.
DR PRIDE; P38110; -.
DR EnsemblFungi; YBL088C_mRNA; YBL088C; YBL088C.
DR GeneID; 852190; -.
DR KEGG; sce:YBL088C; -.
DR SGD; S000000184; TEL1.
DR VEuPathDB; FungiDB:YBL088C; -.
DR eggNOG; KOG0892; Eukaryota.
DR GeneTree; ENSGT00940000174195; -.
DR HOGENOM; CLU_000178_8_1_1; -.
DR InParanoid; P38110; -.
DR OMA; LDKFCGL; -.
DR BioCyc; YEAST:G3O-28977-MON; -.
DR Reactome; R-SCE-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-SCE-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SCE-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
DR Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SCE-69541; Stabilization of p53.
DR Reactome; R-SCE-9664873; Pexophagy.
DR PRO; PR:P38110; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38110; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:SGD.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006975; P:DNA damage induced protein phosphorylation; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IGI:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0016572; P:histone phosphorylation; IEA:InterPro.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR InterPro; IPR015519; ATM/Tel1.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR InterPro; IPR021668; TAN.
DR PANTHER; PTHR11139:SF72; PTHR11139:SF72; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF11640; TAN; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01342; TAN; 1.
DR SUPFAM; SSF56112; SSF56112; 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 3D-structure; ATP-binding; Chromatin regulator; Chromosome; DNA damage;
KW Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Telomere; Transferase.
FT CHAIN 1..2787
FT /note="Serine/threonine-protein kinase TEL1"
FT /id="PRO_0000088839"
FT DOMAIN 1734..2326
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2434..2746
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2755..2787
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2440..2446
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2609..2617
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2629..2653
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MUTAGEN 1319
FT /note="E->K: In TEL1-11; short telomere phenotype and
FT impairs DNA-damage checkpoint function at 37 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:16228207"
FT MUTAGEN 2611..2612
FT /note="GD->DA: Short telomere phenotype in vivo and impairs
FT kinase activity in vitro; when associated with K-2616 and
FT E-2631."
FT /evidence="ECO:0000269|PubMed:11095737,
FT ECO:0000269|PubMed:7671310"
FT MUTAGEN 2616
FT /note="N->K: Short telomere phenotype in vivo and impairs
FT kinase activity in vitro; when associated with D-2611-2612-
FT A and E-2631."
FT /evidence="ECO:0000269|PubMed:11095737,
FT ECO:0000269|PubMed:7671310"
FT MUTAGEN 2631
FT /note="D->E: Short telomere phenotype in vivo and impairs
FT kinase activity in vitro; when associated with D-2611-2612-
FT A and K-2616."
FT /evidence="ECO:0000269|PubMed:11095737,
FT ECO:0000269|PubMed:7671310"
FT CONFLICT 64
FT /note="D -> E (in Ref. 4; AAA69802)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="C -> W (in Ref. 1; CAA56016)"
FT /evidence="ECO:0000305"
FT CONFLICT 1190
FT /note="F -> Y (in Ref. 1; CAA56016)"
FT /evidence="ECO:0000305"
FT CONFLICT 1412
FT /note="C -> F (in Ref. 1; CAA56016 and 2; CAA84909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2787 AA; 321524 MW; C7FA8C6AFD6B04D0 CRC64;
MEDHGIVETL NFLSSTKIKE RNNALDELTT ILKEDPERIP TKALSTTAEA LVELLASEHT
KYCDLLRNLT VSTTNKLSLS ENRLSTISYV LRLFVEKSCE RFKVKTLKLL LAVVPELMVK
DGSKSLLDAV SVHLSFALDA LIKSDPFKLK FMIHQWISLV DKICEYFQSQ MKLSMVDKTL
TNFISILLNL LALDTVGIFQ VTRTITWTVI DFLRLSKKEN GNTRLIMSLI NQLILKCHCF
SVIDTLMLIK EAWSYNLTIG CTSNELVQDQ LSLFDVMSSE LMNHKLPYMI GQENYVEELR
SESLVSLYRE YILLRLSNYK PQLFTVNHVE FSYIRGSRDK NSWFALPDFR LRDRGGRSVW
LKILGITKSL LTYFALNRKN ENYSLLFKRR KCDSDIPSIL RISDDMDTFL IHLLEENSSH
EFEVLGLQLC SFYGTLQDFT KSFAEQLKEL LFSKFEKIQC FNWVCFSFIP LLSQKECELS
NGDMARLFKV CLPLVKSNES CQLSCLLLAN SIKFSKQLLS DEKTINQIYD LYELSDILGP
ILVTNESFML WGYLQYVGKD FQSMNGISSA DRIFEWLKSK WNQLRGTDAK QDQFCNFISW
LGNKYDPENP FNDKKGEGAN PVSLCWDESH KIWQHFQEQR EFLLGVKPEE KSECFNTPFF
NLPKVSLDLT RYNEILYRLL ENIESDAFSS PLQKFTWVAK LIQIVDNLCG DSTFSEFIAA
YKRTTLITIP QLSFDSQNSY QSFFEEVLSI RTINVDHLVL DKINMKEIVN DFIRMQKNKS
QTGTSAINYF EASSEDTTQN NSPYTIGGRF QKPLHSTIDK AVRAYLWSSR NKSISERLVA
ILEFSDCVST DVFISYLGTV CQWLKQAIGE KSSYNKILEE FTEVLGEKLL CNHYSSSNQA
MLLLTSYIEA IRPQWLSYPE QPLNSDCNDI LDWIISRFED NSFTGVAPTV NLSMLLLSLL
QNHDLSHGSI RGGKQRVFAT FIKCLQKLDS SNIINIMNSI SSYMAQVSYK NQSIIFYEIK
SLFGPPQQSI EKSAFYSLAM SMLSLVSYPS LVFSLEDMMT YSGFNHTRAF IQQALNKITV
AFRYQNLTEL FEYCKFDLIM YWFNRTKVPT SKLEKEWDIS LFGFADIHEF LGRYFVEISA
IYFSQGFNQK WILDMLHAIT GNGDAYLVDN SYYLCIPLAF ISGGVNELIF DILPQISGKT
TVKYHKKYRL LMLKWIIRFT DLGSLTELRS TVEKLFPTSY LSPYLFENSS VSMRYQYPLH
IPLALGATLV QTQFAHEKNN THEFKLLFLS VITDLEKTST YIGKLRCARE LKYLFVLYEN
VLVKSSTLNF IIIRLSKFLI DTQIHDEVIT IFSSLLNLAD KNTFEIEPSL PNLFCKIFIY
LRENKQLSPS FQQAIKLLEH RDLIKIKTWK YCLDAIFGNI VQDDIYENTE LLDASDCGVD
DVVLVSLLFS YARRPVASKI GCSLSKAAAI NILKHHVPKE YLSKNFKLWF AALSRRILQQ
EVQRERSTNF NNEVHLKNFE MVFRHPEQPH MIYQRISTFN KEAELYDSTE VFFISECILT
YLVGYSIGNS ESEFCFRDNI MNENKDKVAP LDKDVLNAIY PLANNFGMES FICDTYLSVN
EPYNCWLSKF ARSLIHQISF NIPPIVCLYP LCKGSTAFCE LVLTDLFFLS TTYDPKSCLN
WSNRIFTQIA MLLHVKDSEI KLKMLFNVIK MIRMGSRCKE RNCLRIYSSL DLQEICQISL
KIKEFKFGYL LFEEMNMPNI REMNINTLQK IYECINDGDF LAGLPVPHSI EGVLNSINRI
DSDTWKRFLF NNADFDANYT TSLEEEKESL IKATEDSGFY GLTSLLESRL SGSSDVYKWN
LELGDWKLLT PKVVDSKAKG LYYAIKNLPQ DVGFAEKSLE KSLLTIFDSR QHFISQTEWM
DTLNAIIEFI KIAAIPQDVT SFPQTLMSIM KADKERLNTI DFYDHKTTLK SRHTLMNVLS
RNSLDENVKC SKYLRLGSII QLANYVQLAI ANGAPQDALR NATLMSKTVK NIAKLYDDPS
VVSQIEKLAS FTSANALWES REYKAPVMIM RDLLAQNEKN ISESILYDDF KLLINVPMDQ
IKARLVKWSS ESRLEPAAAI YEKIIVNWDI NVEDHESCSD VFYTLGSFLD EQAQKLRSNG
EIEDREHRSY TGKSTLKALE LIYKNTKLPE NERKDAKRHY NRVLLQYNRD SEVLKALLLQ
KEKFLWHALH FYLNTLVFSN RYDNDIIDKF CGLWFENDDN SKINQLLYKE IGTIPSWKFL
PWVNQIASKI SMEENEFQKP LQLTMKRLLY KLPYDSLYSV MSILLYEKQS NKDTNISQKI
QAVKKILLEL QGYDRGAFAK KYLLPVQEFC EMSVELANLK FVQNTKTLRL ANLKIGQYWL
KQLNMEKLPL PTSNFTVKSS ADGRKARPYI VSVNETVGIT TTGLSLPKIV TFNISDGTTQ
KALMKGSNDD LRQDAIMEQV FQQVNKVLQN DKVLRNLDLG IRTYKVVPLG PKAGIIEFVA
NSTSLHQILS KLHTNDKITF DQARKGMKAV QTKSNEERLK AYLKITNEIK PQLRNFFFDS
FPDPLDWFEA KKTYTKGVAA SSIVGYILGL GDRHLNNILL DCSTGEPIHI DLGIAFDQGK
LLPIPELVPF RLTRDIVDGF GVTGVDGLFR RSCERVYAVL RKDYVKVMCV LNILKWDPLY
SWVMSPVKKY EHLFEEEHEI TNFDNVSKFI SNNDRNENQE SYRALKGVEE KLMGNGLSVE
SSVQDLIQQA TDPSNLSVIY MGWSPFY
