GenomeNet

Database: UniProt
Entry: P38111
LinkDB: P38111
Original site: P38111 
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-OCT-2014, entry version 136.
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; 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
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;
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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
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   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
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. {ECO:0000269|PubMed:11095737,
CC       ECO:0000269|PubMed:11140636, ECO:0000269|PubMed:11359899,
CC       ECO:0000269|PubMed:12181334, ECO:0000269|PubMed:12792653,
CC       ECO:0000269|PubMed:15369670, ECO:0000269|PubMed:15458641,
CC       ECO:0000269|PubMed:15975089, ECO:0000269|PubMed:16148046,
CC       ECO:0000269|PubMed:16365046, ECO:0000269|PubMed:8065923,
CC       ECO:0000269|PubMed:8553072}.
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. {ECO:0000269|PubMed:10950868,
CC       ECO:0000269|PubMed:11060031, ECO:0000269|PubMed:11359899,
CC       ECO:0000269|PubMed:16148046}.
CC   -!- INTERACTION:
CC       P47027:DPB11; NbExp=2; IntAct=EBI-6668, EBI-25984;
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       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 FAT domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00534}.
CC   -!- SIMILARITY: Contains 1 FATC domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00535}.
CC   -!- SIMILARITY: Contains 5 HEAT repeats. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PI3K/PI4K domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00269}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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   BioGrid; 32836; 203.
DR   DIP; DIP-799N; -.
DR   IntAct; P38111; 17.
DR   MINT; MINT-659495; -.
DR   STRING; 4932.YBR136W; -.
DR   MaxQB; P38111; -.
DR   PaxDb; P38111; -.
DR   PeptideAtlas; P38111; -.
DR   EnsemblFungi; YBR136W; YBR136W; YBR136W.
DR   GeneID; 852433; -.
DR   KEGG; sce:YBR136W; -.
DR   CYGD; YBR136w; -.
DR   SGD; S000000340; MEC1.
DR   eggNOG; COG5032; -.
DR   GeneTree; ENSGT00720000108767; -.
DR   HOGENOM; HOG000034220; -.
DR   KO; K02543; -.
DR   OMA; IETIMYD; -.
DR   OrthoDB; EOG7ZWD92; -.
DR   BioCyc; YEAST:G3O-29090-MONOMER; -.
DR   NextBio; 971318; -.
DR   PRO; PR:P38111; -.
DR   Genevestigator; P38111; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IC:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
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; IEA:InterPro.
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:0016572; P:histone phosphorylation; IMP:SGD.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IGI:SGD.
DR   GO; GO:2000105; P:positive regulation of DNA-dependent DNA replication; IMP:SGD.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
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; -; 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; SSF48371; 3.
DR   SUPFAM; SSF56112; SSF56112; 2.
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   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   2368       Serine/threonine-protein kinase MEC1.
FT                                /FTId=PRO_0000088836.
FT   DOMAIN     1399   1944       FAT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00534}.
FT   DOMAIN     2082   2368       PI3K/PI4K. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00269}.
FT   DOMAIN     2336   2368       FATC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00534, ECO:0000255|PROSITE-
FT                                ProRule:PRU00535}.
FT   REGION     2140   2368       Binding to the RPA complex.
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                                {ECO:0000269|PubMed:11359899,
FT                                ECO:0000269|PubMed:16148046}.
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                                {ECO:0000269|PubMed:11359899,
FT                                ECO:0000269|PubMed:16148046}.
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                                {ECO:0000269|PubMed:11359899,
FT                                ECO:0000269|PubMed:16148046}.
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                                {ECO:0000269|PubMed:11359899,
FT                                ECO:0000269|PubMed:16148046}.
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                                {ECO:0000269|PubMed:11359899,
FT                                ECO:0000269|PubMed:16148046}.
FT   MUTAGEN    2224   2224       D->A: Impairs kinase activity; when
FT                                associated with K-2229.
FT                                {ECO:0000269|PubMed:11095737,
FT                                ECO:0000269|PubMed:11359899,
FT                                ECO:0000269|PubMed:16148046}.
FT   MUTAGEN    2229   2229       N->K: Impairs kinase activity; when
FT                                associated with A-2224.
FT                                {ECO:0000269|PubMed:11095737,
FT                                ECO:0000269|PubMed:16148046}.
FT   MUTAGEN    2243   2243       D->E: Impairs kinase activity.
FT                                {ECO:0000269|PubMed:11359899,
FT                                ECO:0000269|PubMed:16148046}.
FT   MUTAGEN    2360   2362       MYI->AAA: In MEC1-85; disrupts
FT                                interaction with RFA1 and severely
FT                                impairs kinase activity.
FT                                {ECO:0000269|PubMed:16148046}.
FT   MUTAGEN    2367   2368       FW->AA: In MEC1-87; decreases the level
FT                                of MEC1 and impairs viability.
FT                                {ECO:0000269|PubMed:16148046}.
FT   CONFLICT    197    197       N -> D (in Ref. 1; BAA01860).
FT                                {ECO:0000305}.
FT   CONFLICT    716    716       S -> P (in Ref. 2; AAA74482).
FT                                {ECO:0000305}.
FT   CONFLICT   1255   1255       K -> Q (in Ref. 2; AAA74482).
FT                                {ECO:0000305}.
FT   CONFLICT   1276   1276       L -> G (in Ref. 2; AAA74482).
FT                                {ECO:0000305}.
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
//
DBGET integrated database retrieval system