ID   RAP1_YEAST              Reviewed;         827 AA.
AC   P11938; D6W0X4;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   27-MAR-2024, entry version 224.
DE   RecName: Full=DNA-binding protein RAP1;
DE   AltName: Full=Repressor/activator site-binding protein;
DE   AltName: Full=SBF-E;
DE   AltName: Full=TUF;
GN   Name=RAP1; Synonyms=GRF1, TUF1; OrderedLocusNames=YNL216W;
GN   ORFNames=N1310;
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=BJ2168;
RX   PubMed=3315231; DOI=10.1016/0092-8674(87)90095-x;
RA   Shore D., Nasmyth K.;
RT   "Purification and cloning of a DNA binding protein from yeast that binds to
RT   both silencer and activator elements.";
RL   Cell 51:721-732(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=7762305; DOI=10.1002/yea.320110111;
RA   Coster F., van Dyck L., Jonniaux J.-L., Purnelle B., Goffeau A.;
RT   "The sequence of a 13.5 kb DNA segment from the left arm of yeast
RT   chromosome XIV reveals MER1; RAP1; a new putative member of the DNA
RT   replication complex and a new putative serine/threonine phosphatase gene.";
RL   Yeast 11:85-91(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [4]
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   [5]
RP   INTERACTION WITH GCR1.
RX   PubMed=8508768; DOI=10.1002/j.1460-2075.1993.tb05897.x;
RA   Tornow J., Zeng X., Gao W., Santangelo G.M.;
RT   "GCR1, a transcriptional activator in Saccharomyces cerevisiae, complexes
RT   with RAP1 and can function without its DNA binding domain.";
RL   EMBO J. 12:2431-2437(1993).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=8194531; DOI=10.1002/j.1460-2075.1994.tb06526.x;
RA   Giraldo R., Rhodes D.;
RT   "The yeast telomere-binding protein RAP1 binds to and promotes the
RT   formation of DNA quadruplexes in telomeric DNA.";
RL   EMBO J. 13:2411-2420(1994).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-486, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-731, AND IDENTIFICATION BY
RP   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).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 360-600.
RX   PubMed=8620531; DOI=10.1016/s0092-8674(00)81088-0;
RA   Koenig P., Giraldo R., Chapman L., Rhodes D.;
RT   "The crystal structure of the DNA-binding domain of yeast RAP1 in complex
RT   with telomeric DNA.";
RL   Cell 85:125-136(1996).
CC   -!- FUNCTION: Essential regulatory protein in yeast whose DNA-binding sites
CC       are found at three types of chromosomal elements: promoters, silencers,
CC       and telomeres. RAP1 is also involved in the regulation of telomere
CC       structure, where its binding sites are found within the terminal
CC       poly[C(1-3)A] sequences. The opposite regulatory functions of RAP1 are
CC       not intrinsic to its binding sites but, instead, result from
CC       interactions with different factors at promoters and silencers. RAP1
CC       associates with SIR3 and SIR4 proteins to form a DNA-binding complex
CC       that initiates the repression at the HM loci and telomeres. May also
CC       target the binding of RIF1 and RIF2 to silencers and telomeres. Forms
CC       with GCR1 a transcriptional activation complex that is required for
CC       expression of glycolytic and ribosomal gene.
CC   -!- SUBUNIT: RIF1, SIR3 and SIR4 associate with RAP1 C-terminus in vivo.
CC       Interacts with a GCR1 homodimer. {ECO:0000269|PubMed:8508768}.
CC   -!- INTERACTION:
CC       P11938; Q08649: ESA1; NbExp=6; IntAct=EBI-14821, EBI-6648;
CC       P11938; P03069: GCN4; NbExp=5; IntAct=EBI-14821, EBI-7450;
CC       P11938; P07261: GCR1; NbExp=2; IntAct=EBI-14821, EBI-7463;
CC       P11938; P29539: RIF1; NbExp=3; IntAct=EBI-14821, EBI-2083307;
CC       P11938; Q06208: RIF2; NbExp=5; IntAct=EBI-14821, EBI-15199;
CC       P11938; P06701: SIR3; NbExp=8; IntAct=EBI-14821, EBI-17230;
CC       P11938; P11978: SIR4; NbExp=4; IntAct=EBI-14821, EBI-17237;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96TL7}.
CC       Chromosome, telomere {ECO:0000250|UniProtKB:Q96TL7}.
CC   -!- MISCELLANEOUS: Present with 4390 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the RAP1 family. {ECO:0000305}.
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DR   EMBL; M18068; AAA18404.1; -; Unassigned_DNA.
DR   EMBL; X78898; CAA55491.1; -; Genomic_DNA.
DR   EMBL; Z71492; CAA96118.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10340.1; -; Genomic_DNA.
DR   PIR; S50714; S50714.
DR   RefSeq; NP_014183.1; NM_001183054.1.
DR   PDB; 1IGN; X-ray; 2.25 A; A/B=353-598.
DR   PDB; 2L42; NMR; -; A=116-212.
DR   PDB; 3CZ6; X-ray; 1.85 A; A/B=672-827.
DR   PDB; 3OWT; X-ray; 2.00 A; A/B=672-827.
DR   PDB; 3UKG; X-ray; 2.95 A; A=360-601.
DR   PDB; 4BJ5; X-ray; 3.29 A; C/E=627-827.
DR   PDB; 4BJ6; X-ray; 3.26 A; C/E=627-827.
DR   PDB; 4BJT; X-ray; 1.61 A; A/B/C=627-827.
DR   PDB; 4GFB; X-ray; 2.99 A; A=358-602.
DR   PDB; 6LDM; X-ray; 2.40 A; A=353-598.
DR   PDBsum; 1IGN; -.
DR   PDBsum; 2L42; -.
DR   PDBsum; 3CZ6; -.
DR   PDBsum; 3OWT; -.
DR   PDBsum; 3UKG; -.
DR   PDBsum; 4BJ5; -.
DR   PDBsum; 4BJ6; -.
DR   PDBsum; 4BJT; -.
DR   PDBsum; 4GFB; -.
DR   PDBsum; 6LDM; -.
DR   AlphaFoldDB; P11938; -.
DR   BMRB; P11938; -.
DR   SMR; P11938; -.
DR   BioGRID; 35620; 709.
DR   ComplexPortal; CPX-1200; RAP1-GCR1 transcription activation complex.
DR   ComplexPortal; CPX-1229; RAP1-GCR1-GCR2 transcription activation complex.
DR   ComplexPortal; CPX-2112; Telosome.
DR   DIP; DIP-851N; -.
DR   IntAct; P11938; 50.
DR   MINT; P11938; -.
DR   STRING; 4932.YNL216W; -.
DR   iPTMnet; P11938; -.
DR   MaxQB; P11938; -.
DR   PaxDb; 4932-YNL216W; -.
DR   PeptideAtlas; P11938; -.
DR   EnsemblFungi; YNL216W_mRNA; YNL216W; YNL216W.
DR   GeneID; 855505; -.
DR   KEGG; sce:YNL216W; -.
DR   AGR; SGD:S000005160; -.
DR   SGD; S000005160; RAP1.
DR   VEuPathDB; FungiDB:YNL216W; -.
DR   eggNOG; ENOG502S85C; Eukaryota.
DR   HOGENOM; CLU_014729_0_0_1; -.
DR   InParanoid; P11938; -.
DR   OMA; TENAWRD; -.
DR   OrthoDB; 1406561at2759; -.
DR   BioCyc; YEAST:G3O-33222-MONOMER; -.
DR   BioGRID-ORCS; 855505; 9 hits in 13 CRISPR screens.
DR   EvolutionaryTrace; P11938; -.
DR   PRO; PR:P11938; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P11938; Protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0000228; C:nuclear chromosome; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
DR   GO; GO:0070187; C:shelterin complex; IDA:SGD.
DR   GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR   GO; GO:0003691; F:double-stranded telomeric DNA binding; IMP:CAFA.
DR   GO; GO:0051880; F:G-quadruplex DNA binding; IDA:SGD.
DR   GO; GO:0042393; F:histone binding; IDA:SGD.
DR   GO; GO:0031492; F:nucleosomal DNA binding; IDA:SGD.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR   GO; GO:0017025; F:TBP-class protein binding; IDA:SGD.
DR   GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR   GO; GO:0001094; F:TFIID-class transcription factor complex binding; IDA:SGD.
DR   GO; GO:0071169; P:establishment of protein localization to chromatin; IPI:SGD.
DR   GO; GO:0070200; P:establishment of protein localization to telomere; IPI:SGD.
DR   GO; GO:0071919; P:G-quadruplex DNA formation; IDA:CACAO.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0060963; P:positive regulation of ribosomal protein gene transcription by RNA polymerase II; NAS:ComplexPortal.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0031848; P:protection from non-homologous end joining at telomere; IMP:SGD.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0006110; P:regulation of glycolytic process; NAS:ComplexPortal.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IGI:SGD.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IGI:SGD.
DR   GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR   GO; GO:0010833; P:telomere maintenance via telomere lengthening; IDA:SGD.
DR   CDD; cd11655; rap1_myb-like; 2.
DR   CDD; cd11653; rap1_RCT; 1.
DR   DisProt; DP00020; -.
DR   Gene3D; 1.10.10.2170; -; 1.
DR   Gene3D; 1.20.120.1480; -; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   IDEAL; IID50071; -.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR021661; Rap1_C.
DR   InterPro; IPR038104; Rap1_C_sf.
DR   InterPro; IPR015280; Rap1_DNA-bd.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR039595; TE2IP/Rap1.
DR   PANTHER; PTHR16466; TELOMERE REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR16466:SF6; TELOMERIC REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   Pfam; PF09197; Rap1-DNA-bind; 1.
DR   Pfam; PF11626; Rap1_C; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS51294; HTH_MYB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Chromosome; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Telomere; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..827
FT                   /note="DNA-binding protein RAP1"
FT                   /id="PRO_0000197112"
FT   DOMAIN          121..208
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   DOMAIN          355..415
FT                   /note="HTH myb-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        388..411
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          29..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..695
FT                   /note="Activation domain"
FT   COMPBIAS        31..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         486
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         731
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CONFLICT        672
FT                   /note="A -> R (in Ref. 1; AAA18404)"
FT                   /evidence="ECO:0000305"
FT   HELIX           365..376
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   HELIX           379..381
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   HELIX           386..391
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   TURN            392..394
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   HELIX           400..409
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   HELIX           412..414
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   STRAND          437..440
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   HELIX           451..470
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   STRAND          474..476
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   STRAND          509..511
FT                   /evidence="ECO:0007829|PDB:3UKG"
FT   HELIX           525..532
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   TURN            533..535
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   HELIX           538..547
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   HELIX           549..552
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   HELIX           554..562
FT                   /evidence="ECO:0007829|PDB:1IGN"
FT   STRAND          566..568
FT                   /evidence="ECO:0007829|PDB:6LDM"
FT   TURN            595..597
FT                   /evidence="ECO:0007829|PDB:3UKG"
FT   HELIX           681..684
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   HELIX           688..690
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   TURN            700..702
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   HELIX           705..708
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   HELIX           713..724
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   TURN            730..732
FT                   /evidence="ECO:0007829|PDB:4BJ6"
FT   HELIX           733..744
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   HELIX           748..757
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   TURN            758..760
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   HELIX           762..764
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   HELIX           765..775
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   STRAND          781..783
FT                   /evidence="ECO:0007829|PDB:4BJ6"
FT   HELIX           789..796
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   HELIX           800..810
FT                   /evidence="ECO:0007829|PDB:4BJT"
FT   HELIX           812..823
FT                   /evidence="ECO:0007829|PDB:4BJT"
SQ   SEQUENCE   827 AA;  92413 MW;  67C4AFB03B3C0713 CRC64;
     MSSPDDFETA PAEYVDALDP SMVVVDSGSA AVTAPSDSAA EVKANQNEEN TGATAAETSE
     KVDQTEVEKK DDDDTTEVGV TTTTPSIADT AATANIASTS GASVTEPTTD DTAADEKKEQ
     VSGPPLSNMK FYLNRDADAH DSLNDIDQLA RLIRANGGEV LDSKPRESKE NVFIVSPYNH
     TNLPTVTPTY IKACCQSNSL LNMENYLVPY DNFREVVDSR LQEESHSNGV DNSNSNSDNK
     DSIRPKTEII STNTNGATED STSEKVMVDA EQQARLQEQA QLLRQHVSST ASITSGGHND
     LVQIEQPQKD TSNNNNSNVN DEDNDLLTQD NNPQTADEGN ASFQAQRSMI SRGALPSHNK
     ASFTDEEDEF ILDVVRKNPT RRTTHTLYDE ISHYVPNHTG NSIRHRFRVY LSKRLEYVYE
     VDKFGKLVRD DDGNLIKTKV LPPSIKRKFS ADEDYTLAIA VKKQFYRDLF QIDPDTGRSL
     ITDEDTPTAI ARRNMTMDPN HVPGSEPNFA AYRTQSRRGP IAREFFKHFA EEHAAHTENA
     WRDRFRKFLL AYGIDDYISY YEAEKAQNRE PEPMKNLTNR PKRPGVPTPG NYNSAAKRAR
     NYSSQRNVQP TANAASANAA AAAAAAASNS YAIPENELLD EDTMNFISSL KNDLSNISNS
     LPFEYPHEIA EAIRSDFSNE DIYDNIDPDT ISFPPKIATT DLFLPLFFHF GSTRQFMDKL
     HEVISGDYEP SQAEKLVQDL CDETGIRKNF STSILTCLSG DLMVFPRYFL NMFKDNVNPP
     PNVPGIWTHD DDESLKSNDQ EQIRKLVKKH GTGRMEMRKR FFEKDLL
//