ATR_YEAST
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 03-AUG-2022, entry version 199.
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; Saccharomycetes;
OC 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 repair
RT and meiotic recombination in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 22:3104-3112(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7926756; DOI=10.1101/gad.8.6.652;
RA Weinert T.A., Kiser G.L., Hartwell L.H.;
RT "Mitotic checkpoint genes in budding yeast and the dependence of mitosis on
RT 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 13
RT complete open reading frames, of which ten correspond to new genes.";
RL Yeast 10:S1-S11(1994).
RN [4]
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 [5]
RP GENOME REANNOTATION.
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 [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 cell
RT 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 of
RT 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 in
RT 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 cerevisiae
RT 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 MUTAGENESIS
RP OF VAL-225; SER-552; LEU-781; PHE-1179; ASN-1700; ASP-2224 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 hypomorphic
RT mec1 alleles impairing subsets of the DNA damage response 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 checkpoint
RT pathway required for cell cycle arrest during senescence in Saccharomyces
RT 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., 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., 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 [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 synthesis
RT 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 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 inositol
RT 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 to
RT sites of DNA damage.";
RL Mol. Biol. Cell 16:5227-5235(2005).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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 in complex with protein LCD1 by the single-strand-binding
CC protein complex RPA to DNA lesions in order to initiate the DNA repair
CC by homologous recombination, after the MRX-complex and TEL1 are
CC displaced. Phosphorylates LCD1 and RPA2, a subunit of RPA, involved in
CC DNA replication, repair and recombination. Phosphorylates RAD9, CHK1
CC and RAD53, which leads to the activation of the CHK1 and RAD53 kinases
CC involved in DNA damage repair cascade. Phosphorylates histone H2A to
CC form 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 proteins involved in genome stability. Required
CC for cell growth and meiotic recombination.
CC {ECO:0000269|PubMed:11095737, ECO:0000269|PubMed:11140636,
CC ECO:0000269|PubMed:11359899, ECO:0000269|PubMed:12181334,
CC ECO:0000269|PubMed:12792653, ECO:0000269|PubMed:15369670,
CC ECO:0000269|PubMed:15458641, ECO:0000269|PubMed:15975089,
CC ECO:0000269|PubMed:16148046, ECO:0000269|PubMed:16365046,
CC ECO:0000269|PubMed:8065923, 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 LCD1, which is required for localization MEC1
CC to the RPA complex. Interacts directly with the RPA subunits RFA1 and
CC RFA2. {ECO:0000269|PubMed:10950868, ECO:0000269|PubMed:11060031,
CC ECO:0000269|PubMed:11359899, ECO:0000269|PubMed:16148046}.
CC -!- INTERACTION:
CC P38111; P47027: DPB11; NbExp=3; IntAct=EBI-6668, EBI-25984;
CC P38111; Q04377: LCD1; NbExp=10; IntAct=EBI-6668, EBI-35652;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Localizes to nuclear DNA repair
CC foci in response to DNA double strand breaks. The recruitment to DNA
CC lesion sites requires its interaction with LCD1 and the presence of the
CC RPA complex on DNA.
CC -!- DEVELOPMENTAL STAGE: Induced during meiosis.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000305}.
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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 PDB; 5X6O; EM; 3.90 A; C=1-2368.
DR PDB; 6Z2W; EM; 2.82 A; E/F=1-2368.
DR PDB; 6Z2X; EM; 3.20 A; E/F=1-2368.
DR PDB; 6Z3A; EM; 3.80 A; E/F=1-2368.
DR PDBsum; 5X6O; -.
DR PDBsum; 6Z2W; -.
DR PDBsum; 6Z2X; -.
DR PDBsum; 6Z3A; -.
DR AlphaFoldDB; P38111; -.
DR SMR; P38111; -.
DR BioGRID; 32836; 375.
DR ComplexPortal; CPX-3621; ATR-ATRIP DNA damage-sensing kinase complex.
DR DIP; DIP-799N; -.
DR IntAct; P38111; 23.
DR MINT; P38111; -.
DR STRING; 4932.YBR136W; -.
DR iPTMnet; P38111; -.
DR MaxQB; P38111; -.
DR PaxDb; P38111; -.
DR PRIDE; P38111; -.
DR EnsemblFungi; YBR136W_mRNA; YBR136W; YBR136W.
DR GeneID; 852433; -.
DR KEGG; sce:YBR136W; -.
DR SGD; S000000340; MEC1.
DR VEuPathDB; FungiDB:YBR136W; -.
DR eggNOG; KOG0890; Eukaryota.
DR HOGENOM; CLU_000178_4_0_1; -.
DR InParanoid; P38111; -.
DR OMA; YTVYSQM; -.
DR BioCyc; YEAST:G3O-29090-MON; -.
DR PRO; PR:P38111; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38111; protein.
DR GO; GO:0070310; C:ATR-ATRIP complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
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; IBA:GO_Central.
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:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IMP:SGD.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IC:ComplexPortal.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IMP:SGD.
DR GO; GO:2000105; P:positive regulation of DNA-templated DNA replication; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0000723; P:telomere maintenance; IDA:SGD.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
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; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR012993; UME.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF08064; UME; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00802; UME; 1.
DR SUPFAM; SSF48371; SSF48371; 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; DNA damage; DNA repair;
KW Kinase; Meiosis; Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2368
FT /note="Serine/threonine-protein kinase MEC1"
FT /id="PRO_0000088836"
FT DOMAIN 1399..1944
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2049..2352
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2336..2368
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2055..2061
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2140..2368
FT /note="Binding to the RPA complex"
FT REGION 2221..2229
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2241..2265
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MUTAGEN 225
FT /note="V->G: In MEC1-101; impairs both the G1/S and intra-S
FT damage checkpoints but not the G2/M damage checkpoint; when
FT associated with P-552 and S-781."
FT /evidence="ECO:0000269|PubMed:11359899"
FT MUTAGEN 552
FT /note="S->P: In MEC1-101; impairs both the G1/S and intra-S
FT damage checkpoints but not the G2/M damage checkpoint; when
FT associated with S-225 and S-781."
FT /evidence="ECO:0000269|PubMed:11359899"
FT MUTAGEN 781
FT /note="L->S: In MEC1-101; impairs both the G1/S and intra-S
FT damage checkpoints but not the G2/M damage checkpoint; when
FT associated with S-225 and P-552."
FT /evidence="ECO:0000269|PubMed:11359899"
FT MUTAGEN 1179
FT /note="F->S: In MEC1-100; impairs both the G1/S and intra-S
FT damage checkpoints but not the G2/M damage checkpoint; when
FT associated with S-1700."
FT /evidence="ECO:0000269|PubMed:11359899"
FT MUTAGEN 1700
FT /note="N->S: In MEC1-100; impairs both the G1/S and intra-S
FT damage checkpoints but not the G2/M damage checkpoint; when
FT associated with S-1179."
FT /evidence="ECO:0000269|PubMed:11359899"
FT MUTAGEN 2224
FT /note="D->A: Impairs kinase activity; when associated with
FT K-2229."
FT /evidence="ECO:0000269|PubMed:11095737,
FT ECO:0000269|PubMed:11359899"
FT MUTAGEN 2229
FT /note="N->K: Impairs kinase activity; when associated with
FT A-2224."
FT /evidence="ECO:0000269|PubMed:11095737"
FT MUTAGEN 2243
FT /note="D->E: Impairs kinase activity."
FT /evidence="ECO:0000269|PubMed:11359899"
FT MUTAGEN 2360..2362
FT /note="MYI->AAA: In MEC1-85; disrupts interaction with RFA1
FT and severely impairs kinase activity."
FT /evidence="ECO:0000269|PubMed:16148046"
FT MUTAGEN 2367..2368
FT /note="FW->AA: In MEC1-87; decreases the level of MEC1 and
FT impairs viability."
FT /evidence="ECO:0000269|PubMed:16148046"
FT CONFLICT 197
FT /note="N -> D (in Ref. 1; BAA01860)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="S -> P (in Ref. 2; AAA74482)"
FT /evidence="ECO:0000305"
FT CONFLICT 1255
FT /note="K -> Q (in Ref. 2; AAA74482)"
FT /evidence="ECO:0000305"
FT CONFLICT 1276
FT /note="L -> G (in Ref. 2; AAA74482)"
FT /evidence="ECO:0000305"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 85..89
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 99..112
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 130..134
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 144..148
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 172..188
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:6Z2X"
FT HELIX 210..228
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 234..252
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 268..283
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 337..354
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:6Z2X"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 391..402
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 412..418
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 432..444
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 454..470
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:6Z2X"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 512..515
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 517..525
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 526..528
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 532..534
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 537..553
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 570..577
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 582..588
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 589..591
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 592..595
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 599..602
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 607..615
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 624..635
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 640..654
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 659..675
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 681..684
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 685..687
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 688..691
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 694..696
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 699..702
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 703..713
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 719..723
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 725..732
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 741..748
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 751..754
FT /evidence="ECO:0007829|PDB:6Z2X"
FT HELIX 756..764
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 768..777
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 784..792
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:6Z2X"
FT HELIX 810..817
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 828..844
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 845..850
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 856..859
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 866..868
FT /evidence="ECO:0007829|PDB:6Z2X"
FT HELIX 869..877
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 881..891
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 900..915
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 920..924
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 926..938
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 943..955
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 960..962
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 963..965
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 967..975
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 982..997
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1000..1004
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1009..1015
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1018..1020
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1023..1026
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1029..1036
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1044..1047
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1048..1051
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1057..1075
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1091..1104
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1105..1107
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1110..1123
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 1128..1130
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 1138..1140
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 1146..1148
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1149..1162
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1164..1169
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1174..1190
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 1194..1196
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1199..1202
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1207..1213
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1218..1224
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1226..1228
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1250..1252
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1254..1266
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1271..1273
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1278..1282
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1289..1303
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1311..1315
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1316..1327
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 1332..1334
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1338..1369
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 1373..1375
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 1378..1380
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1381..1391
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 1392..1395
FT /evidence="ECO:0007829|PDB:6Z2X"
FT STRAND 1397..1399
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1400..1404
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1405..1408
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1410..1422
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1431..1439
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1440..1443
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1451..1455
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1463..1467
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1468..1472
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1476..1486
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1494..1505
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1509..1513
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1516..1518
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 1520..1523
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1531..1544
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1548..1552
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1554..1558
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1567..1583
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1587..1603
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1609..1611
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1615..1617
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1618..1634
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1639..1652
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1660..1674
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1680..1699
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1703..1710
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1712..1715
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1721..1732
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1735..1746
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1747..1750
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1756..1760
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1761..1772
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1773..1775
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1779..1792
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1798..1815
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1824..1836
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1837..1839
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1845..1847
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1848..1864
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1873..1890
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1895..1900
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1901..1905
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 1913..1915
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1916..1928
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1931..1941
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1949..1962
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 1970..1983
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 1984..1986
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2014..2016
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2020..2023
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2057..2060
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2063..2068
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2074..2082
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2085..2101
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2105..2108
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 2109..2111
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2119..2121
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2127..2131
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2133..2137
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2138..2146
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 2147..2150
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2157..2164
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2169..2180
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 2185..2188
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2189..2191
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2196..2220
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2229..2233
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 2234..2236
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2239..2241
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2250..2252
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2253..2256
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2266..2272
FT /evidence="ECO:0007829|PDB:6Z2W"
FT TURN 2276..2279
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2280..2294
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2296..2303
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2306..2309
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2313..2316
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2317..2328
FT /evidence="ECO:0007829|PDB:6Z2W"
FT STRAND 2332..2334
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2340..2351
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2354..2357
FT /evidence="ECO:0007829|PDB:6Z2W"
FT HELIX 2362..2364
FT /evidence="ECO:0007829|PDB:6Z2X"
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
