RS21A_YEAST
ID RS21A_YEAST Reviewed; 87 AA.
AC P0C0V8; D6VXB8; P05760;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=40S ribosomal protein S21-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=S26;
DE AltName: Full=Small ribosomal subunit protein eS21-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS25;
GN Name=RPS21A {ECO:0000303|PubMed:9559554}; Synonyms=RPS25, RPS25A, RPS26A;
GN OrderedLocusNames=YKR057W;
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 PROTEIN SEQUENCE.
RX PubMed=3910104; DOI=10.1021/bi00346a058;
RA Itoh T., Otaka E., Matsui K.A.;
RT "Primary structures of ribosomal protein YS25 from Saccharomyces cerevisiae
RT and its counterparts from Schizosaccharomyces pombe and rat liver.";
RL Biochemistry 24:7418-7423(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2899871; DOI=10.1093/nar/16.13.6223;
RA Suzuki K., Otaka E.;
RT "Cloning and nucleotide sequence of the gene encoding yeast ribosomal
RT protein YS25.";
RL Nucleic Acids Res. 16:6223-6223(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 NOMENCLATURE, AND SUBUNIT.
RX PubMed=9559554;
RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u;
RA Planta R.J., Mager W.H.;
RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL Yeast 14:471-477(1998).
RN [6]
RP ACETYLATION AT MET-1 BY NATB.
RX PubMed=10601260; DOI=10.1074/jbc.274.52.37035;
RA Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
RT "The action of N-terminal acetyltransferases on yeast ribosomal proteins.";
RL J. Biol. Chem. 274:37035-37040(1999).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14627813; DOI=10.1093/nar/gkg899;
RA Tabb-Massey A., Caffrey J.M., Logsden P., Taylor S., Trent J.O.,
RA Ellis S.R.;
RT "Ribosomal proteins Rps0 and Rps21 of Saccharomyces cerevisiae have
RT overlapping functions in the maturation of the 3' end of 18S rRNA.";
RL Nucleic Acids Res. 31:6798-6805(2003).
RN [10]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22096102; DOI=10.1126/science.1212642;
RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel (PubMed:22096102). eS21 is required for the processing of the
CC 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation
CC of 40S ribosomal subunits. Has a physiological role leading to 18S rRNA
CC stability (PubMed:14627813). {ECO:0000269|PubMed:14627813,
CC ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature yeast
CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC different proteins (encoded by 57 genes). The large 60S subunit
CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14627813, ECO:0000269|PubMed:22096102}.
CC -!- PTM: N-terminally acetylated by acetyltransferase NatB.
CC {ECO:0000269|PubMed:10601260}.
CC -!- DISRUPTION PHENOTYPE: Reduction in growth rate, a decrease in free 40S
CC subunits, an increase in the amount of free 60S subunits and a decrease
CC in polysome size. {ECO:0000269|PubMed:14627813}.
CC -!- MISCELLANEOUS: Present with 27400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS21 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family.
CC {ECO:0000305}.
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DR EMBL; X07811; CAA30671.1; -; Genomic_DNA.
DR EMBL; Z28282; CAA82135.1; -; Genomic_DNA.
DR EMBL; Z28283; CAA82137.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09208.1; -; Genomic_DNA.
DR PIR; S00975; R3BY1E.
DR RefSeq; NP_012983.3; NM_001179847.3.
DR PDB; 3J6X; EM; 6.10 A; 21=1-87.
DR PDB; 3J6Y; EM; 6.10 A; 21=1-87.
DR PDB; 3J77; EM; 6.20 A; 21=1-87.
DR PDB; 3J78; EM; 6.30 A; 21=1-87.
DR PDB; 4U3M; X-ray; 3.00 A; D1/d1=1-87.
DR PDB; 4U3N; X-ray; 3.20 A; D1/d1=1-87.
DR PDB; 4U3U; X-ray; 2.90 A; D1/d1=1-87.
DR PDB; 4U4N; X-ray; 3.10 A; D1/d1=1-87.
DR PDB; 4U4O; X-ray; 3.60 A; D1/d1=1-87.
DR PDB; 4U4Q; X-ray; 3.00 A; D1/d1=1-87.
DR PDB; 4U4R; X-ray; 2.80 A; D1/d1=1-87.
DR PDB; 4U4U; X-ray; 3.00 A; D1/d1=1-87.
DR PDB; 4U4Y; X-ray; 3.20 A; D1/d1=1-87.
DR PDB; 4U4Z; X-ray; 3.10 A; D1/d1=1-87.
DR PDB; 4U50; X-ray; 3.20 A; D1/d1=1-87.
DR PDB; 4U51; X-ray; 3.20 A; D1/d1=1-87.
DR PDB; 4U52; X-ray; 3.00 A; D1/d1=1-87.
DR PDB; 4U53; X-ray; 3.30 A; D1/d1=1-87.
DR PDB; 4U55; X-ray; 3.20 A; D1/d1=1-87.
DR PDB; 4U56; X-ray; 3.45 A; D1/d1=1-87.
DR PDB; 4U6F; X-ray; 3.10 A; D1/d1=1-87.
DR PDB; 4V6I; EM; 8.80 A; AT=1-87.
DR PDB; 4V88; X-ray; 3.00 A; AV/CV=1-87.
DR PDB; 4V8Y; EM; 4.30 A; AV=1-87.
DR PDB; 4V8Z; EM; 6.60 A; AV=1-87.
DR PDB; 4V92; EM; 3.70 A; V=1-87.
DR PDB; 5DAT; X-ray; 3.15 A; D1/d1=1-87.
DR PDB; 5DC3; X-ray; 3.25 A; D1/d1=1-87.
DR PDB; 5DGE; X-ray; 3.45 A; D1/d1=1-87.
DR PDB; 5DGF; X-ray; 3.30 A; D1/d1=1-87.
DR PDB; 5DGV; X-ray; 3.10 A; D1/d1=1-87.
DR PDB; 5FCI; X-ray; 3.40 A; D1/d1=1-87.
DR PDB; 5FCJ; X-ray; 3.10 A; D1/d1=1-87.
DR PDB; 5I4L; X-ray; 3.10 A; D1/d1=1-87.
DR PDB; 5JUO; EM; 4.00 A; SB=1-87.
DR PDB; 5JUP; EM; 3.50 A; SB=1-87.
DR PDB; 5JUS; EM; 4.20 A; SB=1-87.
DR PDB; 5JUT; EM; 4.00 A; SB=1-87.
DR PDB; 5JUU; EM; 4.00 A; SB=1-87.
DR PDB; 5LL6; EM; 3.90 A; a=1-87.
DR PDB; 5LYB; X-ray; 3.25 A; D1/d1=1-87.
DR PDB; 5M1J; EM; 3.30 A; V2=1-87.
DR PDB; 5MC6; EM; 3.80 A; a=1-87.
DR PDB; 5MEI; X-ray; 3.50 A; W/d1=1-87.
DR PDB; 5NDG; X-ray; 3.70 A; D1/d1=1-87.
DR PDB; 5NDV; X-ray; 3.30 A; D1/d1=1-87.
DR PDB; 5NDW; X-ray; 3.70 A; D1/d1=1-87.
DR PDB; 5OBM; X-ray; 3.40 A; D1/d1=1-87.
DR PDB; 5ON6; X-ray; 3.10 A; W/d1=1-87.
DR PDB; 5TBW; X-ray; 3.00 A; W/d1=1-87.
DR PDB; 5TGA; X-ray; 3.30 A; D1/d1=1-87.
DR PDB; 5TGM; X-ray; 3.50 A; D1/d1=1-87.
DR PDB; 6EML; EM; 3.60 A; a=1-87.
DR PDB; 6FAI; EM; 3.40 A; V=1-87.
DR PDB; 6GQ1; EM; 4.40 A; AL=1-87.
DR PDB; 6GQB; EM; 3.90 A; AL=1-87.
DR PDB; 6GQV; EM; 4.00 A; AL=1-87.
DR PDB; 6HHQ; X-ray; 3.10 A; W/d1=1-87.
DR PDB; 6I7O; EM; 5.30 A; a/ab=1-87.
DR PDB; 6Q8Y; EM; 3.10 A; a=1-87.
DR PDB; 6RBD; EM; 3.47 A; V=1-87.
DR PDB; 6RBE; EM; 3.80 A; V=1-87.
DR PDB; 6S47; EM; 3.28 A; BW=1-87.
DR PDB; 6SNT; EM; 2.80 A; V=1-87.
DR PDB; 6SV4; EM; 3.30 A; a/ab/ac=1-87.
DR PDB; 6T4Q; EM; 2.60 A; SV=1-87.
DR PDB; 6T7I; EM; 3.20 A; SV=1-87.
DR PDB; 6T7T; EM; 3.10 A; SV=1-87.
DR PDB; 6T83; EM; 4.00 A; Vb/w=1-87.
DR PDB; 6TB3; EM; 2.80 A; a=1-87.
DR PDB; 6TNU; EM; 3.10 A; a=1-87.
DR PDB; 6WDR; EM; 3.70 A; V=1-87.
DR PDB; 6WOO; EM; 2.90 A; VV=1-87.
DR PDB; 6XIQ; EM; 4.20 A; AL=1-87.
DR PDB; 6XIR; EM; 3.20 A; AL=1-87.
DR PDB; 6Y7C; EM; 3.80 A; V=1-87.
DR PDB; 6Z6J; EM; 3.40 A; SV=1-87.
DR PDB; 6Z6K; EM; 3.40 A; SV=1-87.
DR PDB; 6ZCE; EM; 5.30 A; W=1-87.
DR PDB; 6ZU9; EM; 6.20 A; a=1-87.
DR PDB; 6ZVI; EM; 3.00 A; D=1-87.
DR PDB; 7A1G; EM; 3.00 A; a=1-87.
DR PDB; 7B7D; EM; 3.30 A; a=1-87.
DR PDB; 7NRC; EM; 3.90 A; Sa=1-87.
DR PDB; 7NRD; EM; 4.36 A; Sa=1-87.
DR PDB; 7RR5; EM; 3.23 A; SV=1-87.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 4U3M; -.
DR PDBsum; 4U3N; -.
DR PDBsum; 4U3U; -.
DR PDBsum; 4U4N; -.
DR PDBsum; 4U4O; -.
DR PDBsum; 4U4Q; -.
DR PDBsum; 4U4R; -.
DR PDBsum; 4U4U; -.
DR PDBsum; 4U4Y; -.
DR PDBsum; 4U4Z; -.
DR PDBsum; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LL6; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5M1J; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WDR; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6XIQ; -.
DR PDBsum; 6XIR; -.
DR PDBsum; 6Y7C; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7RR5; -.
DR AlphaFoldDB; P0C0V8; -.
DR SMR; P0C0V8; -.
DR BioGRID; 34188; 258.
DR IntAct; P0C0V8; 11.
DR MINT; P0C0V8; -.
DR STRING; 4932.YKR057W; -.
DR iPTMnet; P0C0V8; -.
DR UCD-2DPAGE; P0C0V8; -.
DR MaxQB; P0C0V8; -.
DR PaxDb; P0C0V8; -.
DR PRIDE; P0C0V8; -.
DR TopDownProteomics; P0C0V8; -.
DR EnsemblFungi; YKR057W_mRNA; YKR057W; YKR057W.
DR GeneID; 853931; -.
DR KEGG; sce:YKR057W; -.
DR SGD; S000001765; RPS21A.
DR VEuPathDB; FungiDB:YKR057W; -.
DR eggNOG; KOG3486; Eukaryota.
DR GeneTree; ENSGT00390000017515; -.
DR HOGENOM; CLU_167122_2_0_1; -.
DR InParanoid; P0C0V8; -.
DR OMA; AMDRLWQ; -.
DR BioCyc; YEAST:G3O-32026-MON; -.
DR PRO; PR:P0C0V8; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P0C0V8; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000461; P:endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR Gene3D; 3.30.1230.20; -; 1.
DR InterPro; IPR001931; Ribosomal_S21e.
DR InterPro; IPR018279; Ribosomal_S21e_CS.
DR InterPro; IPR038579; Ribosomal_S21e_sf.
DR PANTHER; PTHR10442; PTHR10442; 1.
DR Pfam; PF01249; Ribosomal_S21e; 1.
DR PIRSF; PIRSF002148; Ribosomal_S21e; 1.
DR PROSITE; PS00996; RIBOSOMAL_S21E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; rRNA processing.
FT CHAIN 1..87
FT /note="40S ribosomal protein S21-A"
FT /id="PRO_0000194761"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:10601260"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:7A1G"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:7A1G"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 87 AA; 9746 MW; 52E1C24744E24F80 CRC64;
MENDKGQLVE LYVPRKCSAT NRIIKADDHA SVQINVAKVD EEGRAIPGEY VTYALSGYVR
SRGESDDSLN RLAQNDGLLK NVWSYSR
