RS27A_YEAST
ID RS27A_YEAST Reviewed; 82 AA.
AC P35997; D6VX42;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=40S ribosomal protein S27-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP61;
DE AltName: Full=Small ribosomal subunit protein eS27-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YS20;
GN Name=RPS27A {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YKL156W;
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=8091859; DOI=10.1002/yea.320100005;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci
RT of chromosome XI of Saccharomyces cerevisiae.";
RL Yeast 10:S35-S40(1994).
RN [2]
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 [3]
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 [4]
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 [5]
RP ANALYSIS OF N-TERMINUS.
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 [6]
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 [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 METHYLATION AT CYS-40.
RX PubMed=22650761; DOI=10.1021/bi300186g;
RA Young B.D., Weiss D.I., Zurita-Lopez C.I., Webb K.J., Clarke S.G.,
RA McBride A.E.;
RT "Identification of methylated proteins in the yeast small ribosomal
RT subunit: a role for SPOUT methyltransferases in protein arginine
RT methylation.";
RL Biochemistry 51:5091-5104(2012).
RN [9]
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 [10]
RP STRUCTURE BY ELECTRON MICROSCOPY.
RX PubMed=20980660; DOI=10.1073/pnas.1009999107;
RA Armache J.P., Jarasch A., Anger A.M., Villa E., Becker T., Bhushan S.,
RA Jossinet F., Habeck M., Dindar G., Franckenberg S., Marquez V., Mielke T.,
RA Thomm M., Berninghausen O., Beatrix B., Soding J., Westhof E., Wilson D.N.,
RA Beckmann R.;
RT "Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome
RT at 5.5-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19748-19753(2010).
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).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS).
RX PubMed=24200810; DOI=10.1126/science.1240585;
RA Fernandez I.S., Bai X.C., Hussain T., Kelley A.C., Lorsch J.R.,
RA Ramakrishnan V., Scheres S.H.;
RT "Molecular architecture of a eukaryotic translational initiation complex.";
RL Science 342:1240585-1240585(2013).
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. {ECO:0000305|PubMed:22096102}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
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:22096102}.
CC -!- PTM: The N-terminus is not modified. {ECO:0000269|PubMed:10601260}.
CC -!- MISCELLANEOUS: Present with 43300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS27 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS27 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z26877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z28156; CAA81998.1; -; Genomic_DNA.
DR EMBL; Z28155; CAA81997.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09008.1; -; Genomic_DNA.
DR PIR; S37986; S37986.
DR RefSeq; NP_012766.1; NM_001179722.1.
DR PDB; 3J6X; EM; 6.10 A; 27=1-82.
DR PDB; 3J6Y; EM; 6.10 A; 27=1-82.
DR PDB; 3J77; EM; 6.20 A; 27=1-82.
DR PDB; 3J78; EM; 6.30 A; 27=1-82.
DR PDB; 4U3M; X-ray; 3.00 A; D7/d7=2-82.
DR PDB; 4U3N; X-ray; 3.20 A; D7/d7=2-82.
DR PDB; 4U3U; X-ray; 2.90 A; D7/d7=2-82.
DR PDB; 4U4N; X-ray; 3.10 A; D7/d7=2-82.
DR PDB; 4U4O; X-ray; 3.60 A; D7/d7=2-82.
DR PDB; 4U4Q; X-ray; 3.00 A; D7/d7=2-82.
DR PDB; 4U4R; X-ray; 2.80 A; D7/d7=2-82.
DR PDB; 4U4U; X-ray; 3.00 A; D7/d7=2-82.
DR PDB; 4U4Y; X-ray; 3.20 A; D7/d7=2-82.
DR PDB; 4U4Z; X-ray; 3.10 A; D7/d7=2-82.
DR PDB; 4U50; X-ray; 3.20 A; D7/d7=2-82.
DR PDB; 4U51; X-ray; 3.20 A; D7/d7=2-82.
DR PDB; 4U52; X-ray; 3.00 A; D7/d7=2-82.
DR PDB; 4U53; X-ray; 3.30 A; D7/d7=2-82.
DR PDB; 4U55; X-ray; 3.20 A; D7/d7=2-82.
DR PDB; 4U56; X-ray; 3.45 A; D7/d7=2-82.
DR PDB; 4U6F; X-ray; 3.10 A; D7/d7=2-82.
DR PDB; 4V6I; EM; 8.80 A; AX=1-82.
DR PDB; 4V88; X-ray; 3.00 A; Ab/Cb=1-82.
DR PDB; 4V8Y; EM; 4.30 A; A1=1-82.
DR PDB; 4V8Z; EM; 6.60 A; A1=1-82.
DR PDB; 4V92; EM; 3.70 A; b=2-82.
DR PDB; 5DAT; X-ray; 3.15 A; D7/d7=2-82.
DR PDB; 5DC3; X-ray; 3.25 A; D7/d7=2-82.
DR PDB; 5DGE; X-ray; 3.45 A; D7/d7=2-82.
DR PDB; 5DGF; X-ray; 3.30 A; D7/d7=2-82.
DR PDB; 5DGV; X-ray; 3.10 A; D7/d7=2-82.
DR PDB; 5FCI; X-ray; 3.40 A; D7/d7=2-82.
DR PDB; 5FCJ; X-ray; 3.10 A; D7/d7=2-82.
DR PDB; 5I4L; X-ray; 3.10 A; D7/d7=2-82.
DR PDB; 5JUO; EM; 4.00 A; YB=1-82.
DR PDB; 5JUP; EM; 3.50 A; YB=1-82.
DR PDB; 5JUS; EM; 4.20 A; YB=1-82.
DR PDB; 5JUT; EM; 4.00 A; YB=1-82.
DR PDB; 5JUU; EM; 4.00 A; YB=1-82.
DR PDB; 5LL6; EM; 3.90 A; f=1-82.
DR PDB; 5LYB; X-ray; 3.25 A; D7/d7=2-82.
DR PDB; 5M1J; EM; 3.30 A; b2=2-82.
DR PDB; 5MC6; EM; 3.80 A; f=1-82.
DR PDB; 5MEI; X-ray; 3.50 A; c/d7=2-82.
DR PDB; 5NDG; X-ray; 3.70 A; D7/d7=2-82.
DR PDB; 5NDV; X-ray; 3.30 A; D7/d7=2-82.
DR PDB; 5NDW; X-ray; 3.70 A; D7/d7=2-82.
DR PDB; 5OBM; X-ray; 3.40 A; D7/d7=2-82.
DR PDB; 5ON6; X-ray; 3.10 A; c/d7=2-82.
DR PDB; 5TBW; X-ray; 3.00 A; c/d7=2-82.
DR PDB; 5TGA; X-ray; 3.30 A; D7/d7=2-82.
DR PDB; 5TGM; X-ray; 3.50 A; D7/d7=2-82.
DR PDB; 5WYJ; EM; 8.70 A; Sc=1-82.
DR PDB; 5WYK; EM; 4.50 A; Sc=1-82.
DR PDB; 6EML; EM; 3.60 A; f=1-82.
DR PDB; 6FAI; EM; 3.40 A; b=1-82.
DR PDB; 6GQ1; EM; 4.40 A; AR=2-82.
DR PDB; 6GQB; EM; 3.90 A; AR=2-82.
DR PDB; 6GQV; EM; 4.00 A; AR=2-82.
DR PDB; 6HHQ; X-ray; 3.10 A; c/d7=1-82.
DR PDB; 6I7O; EM; 5.30 A; f/fb=2-82.
DR PDB; 6KE6; EM; 3.40 A; Sc=1-82.
DR PDB; 6LQP; EM; 3.20 A; Sc=1-82.
DR PDB; 6LQQ; EM; 4.10 A; Sc=1-82.
DR PDB; 6LQR; EM; 8.60 A; Sc=1-82.
DR PDB; 6LQS; EM; 3.80 A; Sc=1-82.
DR PDB; 6LQT; EM; 4.90 A; Sc=1-82.
DR PDB; 6Q8Y; EM; 3.10 A; f=2-82.
DR PDB; 6RBD; EM; 3.47 A; b=1-82.
DR PDB; 6RBE; EM; 3.80 A; b=1-82.
DR PDB; 6S47; EM; 3.28 A; Bc=2-82.
DR PDB; 6SNT; EM; 2.80 A; b=1-82.
DR PDB; 6SV4; EM; 3.30 A; f/fb/fc=1-82.
DR PDB; 6T4Q; EM; 2.60 A; Sb=2-82.
DR PDB; 6T7I; EM; 3.20 A; Sb=1-82.
DR PDB; 6T7T; EM; 3.10 A; Sb=1-82.
DR PDB; 6T83; EM; 4.00 A; 2/bb=1-82.
DR PDB; 6TB3; EM; 2.80 A; f=2-82.
DR PDB; 6TNU; EM; 3.10 A; f=2-82.
DR PDB; 6WDR; EM; 3.70 A; b=2-82.
DR PDB; 6WOO; EM; 2.90 A; bb=2-82.
DR PDB; 6XIQ; EM; 4.20 A; AR=1-82.
DR PDB; 6XIR; EM; 3.20 A; AR=1-82.
DR PDB; 6Y7C; EM; 3.80 A; b=1-82.
DR PDB; 6Z6J; EM; 3.40 A; Sb=1-82.
DR PDB; 6Z6K; EM; 3.40 A; Sb=1-82.
DR PDB; 6ZCE; EM; 5.30 A; c=1-82.
DR PDB; 6ZQA; EM; 4.40 A; Db=1-82.
DR PDB; 6ZQB; EM; 3.90 A; Db=1-82.
DR PDB; 6ZQC; EM; 3.80 A; Db=1-82.
DR PDB; 6ZQD; EM; 3.80 A; Db=1-82.
DR PDB; 6ZQE; EM; 7.10 A; Db=1-82.
DR PDB; 6ZQF; EM; 4.90 A; Db=1-82.
DR PDB; 6ZQG; EM; 3.50 A; Db=1-82.
DR PDB; 6ZU9; EM; 6.20 A; f=1-82.
DR PDB; 6ZVI; EM; 3.00 A; L=2-82.
DR PDB; 7A1G; EM; 3.00 A; f=2-82.
DR PDB; 7AJT; EM; 4.60 A; Db=1-82.
DR PDB; 7AJU; EM; 3.80 A; Db=1-82.
DR PDB; 7B7D; EM; 3.30 A; f=2-82.
DR PDB; 7D4I; EM; 4.00 A; Sc=1-82.
DR PDB; 7D5T; EM; 6.00 A; Sc=1-82.
DR PDB; 7D63; EM; 12.30 A; Sc=1-82.
DR PDB; 7NRC; EM; 3.90 A; Sf=2-82.
DR PDB; 7NRD; EM; 4.36 A; Sf=2-82.
DR PDB; 7OSA; X-ray; 3.00 A; eS27=1-82.
DR PDB; 7OSM; X-ray; 3.00 A; eS27=1-82.
DR PDB; 7RR5; EM; 3.23 A; Sb=1-82.
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; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
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; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7OSA; -.
DR PDBsum; 7OSM; -.
DR PDBsum; 7RR5; -.
DR AlphaFoldDB; P35997; -.
DR SMR; P35997; -.
DR BioGRID; 33981; 713.
DR IntAct; P35997; 11.
DR MINT; P35997; -.
DR STRING; 4932.YKL156W; -.
DR iPTMnet; P35997; -.
DR MaxQB; P35997; -.
DR PaxDb; P35997; -.
DR PRIDE; P35997; -.
DR TopDownProteomics; P35997; -.
DR EnsemblFungi; YKL156W_mRNA; YKL156W; YKL156W.
DR GeneID; 853700; -.
DR KEGG; sce:YKL156W; -.
DR SGD; S000001639; RPS27A.
DR VEuPathDB; FungiDB:YKL156W; -.
DR eggNOG; KOG1779; Eukaryota.
DR GeneTree; ENSGT00940000167938; -.
DR HOGENOM; CLU_130128_3_0_1; -.
DR InParanoid; P35997; -.
DR OMA; LHPAIDF; -.
DR BioCyc; YEAST:G3O-31926-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P35997; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P35997; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:SGD.
DR Gene3D; 2.20.25.100; -; 1.
DR HAMAP; MF_00371; Ribosomal_S27e; 1.
DR InterPro; IPR000592; Ribosomal_S27.
DR InterPro; IPR023407; Ribosomal_S27_Zn-bd_dom_sf.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR PANTHER; PTHR11594; PTHR11594; 1.
DR Pfam; PF01667; Ribosomal_S27e; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS01168; RIBOSOMAL_S27E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Methylation; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Zinc; Zinc-finger.
FT CHAIN 1..82
FT /note="40S ribosomal protein S27-A"
FT /id="PRO_0000149066"
FT ZN_FING 37..59
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT MOD_RES 40
FT /note="S-methylcysteine"
FT /evidence="ECO:0000269|PubMed:22650761"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:7A1G"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 82 AA; 8879 MW; FCA80130CFCEC91E CRC64;
MVLVQDLLHP TAASEARKHK LKTLVQGPRS YFLDVKCPGC LNITTVFSHA QTAVTCESCS
TILCTPTGGK AKLSEGTSFR RK
