RS9A_YEAST
ID RS9A_YEAST Reviewed; 197 AA.
AC O13516; D6W3T6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=40S ribosomal protein S9-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP21;
DE AltName: Full=S13;
DE AltName: Full=Small ribosomal subunit protein uS4-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YP28;
DE AltName: Full=YS11;
GN Name=RPS9A {ECO:0000303|PubMed:9559554}; Synonyms=RPS13A, YS11A;
GN OrderedLocusNames=YPL081W;
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].
RX PubMed=2041737; DOI=10.1093/nar/19.10.2603;
RA Mizuta K., Hashimoto T., Suzuki K., Otaka E.;
RT "Yeast ribosomal proteins: XII. YS11 of Saccharomyces cerevisiae is a
RT homologue to E. coli S4 according to the gene analysis.";
RL Nucleic Acids Res. 19:2603-2608(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 PROTEIN SEQUENCE OF 2-24.
RX PubMed=6814480; DOI=10.1021/bi00262a005;
RA Otaka E., Higo K., Osawa S.;
RT "Isolation of seventeen proteins and amino-terminal amino acid sequences of
RT eight proteins from cytoplasmic ribosomes of yeast.";
RL Biochemistry 21:4545-4550(1982).
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 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 FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME, AND SUBCELLULAR LOCATION.
RX PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004;
RA Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S.,
RA Baserga S.J.;
RT "The small-subunit processome is a ribosome assembly intermediate.";
RL Eukaryot. Cell 3:1619-1626(2004).
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 3D-STRUCTURE MODELING OF 19-196, AND ELECTRON MICROSCOPY.
RX PubMed=11701127; DOI=10.1016/s0092-8674(01)00539-6;
RA Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G.,
RA Frank J.;
RT "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-
RT ribosome and subunit-subunit interactions.";
RL Cell 107:373-386(2001).
RN [11]
RP 3D-STRUCTURE MODELING OF 19-197, AND ELECTRON MICROSCOPY.
RX PubMed=14976550; DOI=10.1038/sj.emboj.7600102;
RA Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R.,
RA Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
RT "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome
RT facilitate tRNA translocation.";
RL EMBO J. 23:1008-1019(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=21109664; DOI=10.1126/science.1194294;
RA Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
RT "Crystal structure of the eukaryotic ribosome.";
RL Science 330:1203-1209(2010).
RN [13]
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). uS4 is involved in nucleolar processing of
CC pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).
CC {ECO:0000269|PubMed:15590835, 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 Interacts with snoRNA U3. uS11 interacts with MPP10. Component of the
CC ribosomal small subunit (SSU) processome composed of at least 40
CC protein subunits and snoRNA U3 (PubMed:15590835).
CC {ECO:0000269|PubMed:15590835, ECO:0000269|PubMed:22096102,
CC ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15590835}.
CC -!- MISCELLANEOUS: Present with 106000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uS4 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000305}.
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DR EMBL; D00724; BAA00626.1; -; Genomic_DNA.
DR EMBL; U41849; AAB68268.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11352.1; -; Genomic_DNA.
DR PIR; S16822; S16822.
DR RefSeq; NP_015244.1; NM_001183895.1.
DR PDB; 3J6X; EM; 6.10 A; S9=1-197.
DR PDB; 3J6Y; EM; 6.10 A; S9=1-197.
DR PDB; 3J77; EM; 6.20 A; S9=1-197.
DR PDB; 3J78; EM; 6.30 A; S9=1-197.
DR PDB; 4U3M; X-ray; 3.00 A; S9/s9=2-197.
DR PDB; 4U3N; X-ray; 3.20 A; S9/s9=2-197.
DR PDB; 4U3U; X-ray; 2.90 A; S9/s9=2-197.
DR PDB; 4U4N; X-ray; 3.10 A; S9/s9=2-197.
DR PDB; 4U4O; X-ray; 3.60 A; S9/s9=2-197.
DR PDB; 4U4Q; X-ray; 3.00 A; S9/s9=2-197.
DR PDB; 4U4R; X-ray; 2.80 A; S9/s9=2-197.
DR PDB; 4U4U; X-ray; 3.00 A; S9/s9=2-197.
DR PDB; 4U4Y; X-ray; 3.20 A; S9/s9=2-197.
DR PDB; 4U4Z; X-ray; 3.10 A; S9/s9=2-197.
DR PDB; 4U50; X-ray; 3.20 A; S9/s9=2-197.
DR PDB; 4U51; X-ray; 3.20 A; S9/s9=2-197.
DR PDB; 4U52; X-ray; 3.00 A; S9/s9=2-197.
DR PDB; 4U53; X-ray; 3.30 A; S9/s9=2-197.
DR PDB; 4U55; X-ray; 3.20 A; S9/s9=2-197.
DR PDB; 4U56; X-ray; 3.45 A; S9/s9=2-197.
DR PDB; 4U6F; X-ray; 3.10 A; S9/s9=2-197.
DR PDB; 4V4B; EM; 11.70 A; AD=19-197.
DR PDB; 4V6I; EM; 8.80 A; AC=1-197.
DR PDB; 4V7R; X-ray; 4.00 A; AE/CE=1-197.
DR PDB; 4V88; X-ray; 3.00 A; AJ/CJ=1-197.
DR PDB; 4V8Y; EM; 4.30 A; AJ=1-197.
DR PDB; 4V8Z; EM; 6.60 A; AJ=1-197.
DR PDB; 4V92; EM; 3.70 A; J=2-180.
DR PDB; 5DAT; X-ray; 3.15 A; S9/s9=2-197.
DR PDB; 5DC3; X-ray; 3.25 A; S9/s9=2-197.
DR PDB; 5DGE; X-ray; 3.45 A; S9/s9=2-197.
DR PDB; 5DGF; X-ray; 3.30 A; S9/s9=2-197.
DR PDB; 5DGV; X-ray; 3.10 A; S9/s9=2-197.
DR PDB; 5FCI; X-ray; 3.40 A; S9/s9=2-197.
DR PDB; 5FCJ; X-ray; 3.10 A; S9/s9=2-197.
DR PDB; 5I4L; X-ray; 3.10 A; S9/s9=2-186.
DR PDB; 5JPQ; EM; 7.30 A; u=1-197.
DR PDB; 5JUO; EM; 4.00 A; GB=1-197.
DR PDB; 5JUP; EM; 3.50 A; GB=1-197.
DR PDB; 5JUS; EM; 4.20 A; GB=1-197.
DR PDB; 5JUT; EM; 4.00 A; GB=1-197.
DR PDB; 5JUU; EM; 4.00 A; GB=1-197.
DR PDB; 5LL6; EM; 3.90 A; W=1-197.
DR PDB; 5LYB; X-ray; 3.25 A; S9/s9=2-186.
DR PDB; 5M1J; EM; 3.30 A; J2=2-186.
DR PDB; 5MC6; EM; 3.80 A; W=1-197.
DR PDB; 5MEI; X-ray; 3.50 A; K/s9=2-186.
DR PDB; 5NDG; X-ray; 3.70 A; S9/s9=2-186.
DR PDB; 5NDV; X-ray; 3.30 A; S9/s9=2-186.
DR PDB; 5NDW; X-ray; 3.70 A; S9/s9=2-186.
DR PDB; 5OBM; X-ray; 3.40 A; S9/s9=2-186.
DR PDB; 5ON6; X-ray; 3.10 A; K/s9=2-186.
DR PDB; 5TBW; X-ray; 3.00 A; K/s9=2-186.
DR PDB; 5TGA; X-ray; 3.30 A; S9/s9=2-186.
DR PDB; 5TGM; X-ray; 3.50 A; S9/s9=2-186.
DR PDB; 5TZS; EM; 5.10 A; 9=1-197.
DR PDB; 5WLC; EM; 3.80 A; L9=1-197.
DR PDB; 5WYJ; EM; 8.70 A; SK=1-197.
DR PDB; 5WYK; EM; 4.50 A; SK=1-197.
DR PDB; 6EML; EM; 3.60 A; W=1-197.
DR PDB; 6FAI; EM; 3.40 A; J=1-197.
DR PDB; 6GQ1; EM; 4.40 A; z=2-186.
DR PDB; 6GQB; EM; 3.90 A; z=2-186.
DR PDB; 6GQV; EM; 4.00 A; z=2-186.
DR PDB; 6HHQ; X-ray; 3.10 A; K/s9=1-197.
DR PDB; 6I7O; EM; 5.30 A; W/Wb=2-186.
DR PDB; 6KE6; EM; 3.40 A; SK=1-197.
DR PDB; 6LQP; EM; 3.20 A; SK=1-197.
DR PDB; 6LQQ; EM; 4.10 A; SK=1-197.
DR PDB; 6LQR; EM; 8.60 A; SK=1-197.
DR PDB; 6LQS; EM; 3.80 A; SK=1-197.
DR PDB; 6LQT; EM; 4.90 A; SK=1-197.
DR PDB; 6LQU; EM; 3.70 A; SK=1-197.
DR PDB; 6LQV; EM; 4.80 A; SK=1-197.
DR PDB; 6Q8Y; EM; 3.10 A; W=9-186.
DR PDB; 6RBD; EM; 3.47 A; J=1-197.
DR PDB; 6RBE; EM; 3.80 A; J=1-197.
DR PDB; 6S47; EM; 3.28 A; BK=2-197.
DR PDB; 6SNT; EM; 2.80 A; J=1-197.
DR PDB; 6SV4; EM; 3.30 A; W/Wb/Wc=1-197.
DR PDB; 6T4Q; EM; 2.60 A; SJ=2-185.
DR PDB; 6T7I; EM; 3.20 A; SJ=1-197.
DR PDB; 6T7T; EM; 3.10 A; SJ=1-197.
DR PDB; 6T83; EM; 4.00 A; Jb/k=1-197.
DR PDB; 6TB3; EM; 2.80 A; W=2-185.
DR PDB; 6TNU; EM; 3.10 A; W=2-185.
DR PDB; 6WDR; EM; 3.70 A; J=2-186.
DR PDB; 6XIQ; EM; 4.20 A; z=1-197.
DR PDB; 6XIR; EM; 3.20 A; z=1-197.
DR PDB; 6Y7C; EM; 3.80 A; J=1-197.
DR PDB; 6Z6J; EM; 3.40 A; SJ=1-197.
DR PDB; 6Z6K; EM; 3.40 A; SJ=1-197.
DR PDB; 6ZCE; EM; 5.30 A; K=1-197.
DR PDB; 6ZQA; EM; 4.40 A; DJ=1-197.
DR PDB; 6ZQB; EM; 3.90 A; DJ=1-197.
DR PDB; 6ZQC; EM; 3.80 A; DJ=1-197.
DR PDB; 6ZQD; EM; 3.80 A; DJ=1-197.
DR PDB; 6ZQE; EM; 7.10 A; DJ=1-197.
DR PDB; 6ZQF; EM; 4.90 A; DJ=1-197.
DR PDB; 6ZQG; EM; 3.50 A; DJ=1-197.
DR PDB; 6ZU9; EM; 6.20 A; W=1-197.
DR PDB; 6ZVI; EM; 3.00 A; r=2-186.
DR PDB; 7A1G; EM; 3.00 A; W=2-185.
DR PDB; 7AJT; EM; 4.60 A; DJ=1-197.
DR PDB; 7AJU; EM; 3.80 A; DJ=1-197.
DR PDB; 7B7D; EM; 3.30 A; W=2-185.
DR PDB; 7D4I; EM; 4.00 A; SK=1-197.
DR PDB; 7D5S; EM; 4.60 A; SK=1-197.
DR PDB; 7D5T; EM; 6.00 A; SK=1-197.
DR PDB; 7D63; EM; 12.30 A; SK=1-197.
DR PDB; 7NRC; EM; 3.90 A; SW=2-185.
DR PDB; 7NRD; EM; 4.36 A; SW=2-186.
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; 4V4B; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V7R; -.
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; 5JPQ; -.
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; 5TZS; -.
DR PDBsum; 5WLC; -.
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; 6LQU; -.
DR PDBsum; 6LQV; -.
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; 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; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; O13516; -.
DR SMR; O13516; -.
DR BioGRID; 36100; 688.
DR IntAct; O13516; 35.
DR MINT; O13516; -.
DR STRING; 4932.YPL081W; -.
DR iPTMnet; O13516; -.
DR MaxQB; O13516; -.
DR PaxDb; O13516; -.
DR PRIDE; O13516; -.
DR TopDownProteomics; O13516; -.
DR EnsemblFungi; YPL081W_mRNA; YPL081W; YPL081W.
DR GeneID; 856024; -.
DR KEGG; sce:YPL081W; -.
DR SGD; S000006002; RPS9A.
DR VEuPathDB; FungiDB:YPL081W; -.
DR eggNOG; KOG3301; Eukaryota.
DR GeneTree; ENSGT00550000074829; -.
DR HOGENOM; CLU_089738_0_0_1; -.
DR InParanoid; O13516; -.
DR OMA; ARQFITH; -.
DR BioCyc; YEAST:G3O-33987-MON; -.
DR EvolutionaryTrace; O13516; -.
DR PRO; PR:O13516; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; O13516; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
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:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0019843; F:rRNA binding; 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:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR005710; Ribosomal_S4/S9_euk/arc.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01018; uS4_arch; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ribosome biogenesis; RNA-binding; rRNA processing;
KW rRNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6814480"
FT CHAIN 2..197
FT /note="40S ribosomal protein S9-A"
FT /id="PRO_0000132703"
FT DOMAIN 107..181
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00182"
FT REGION 160..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05755"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P05755"
FT CONFLICT 20..22
FT /note="ESS -> QSB (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 23..26
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 40..61
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 67..82
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:7A1G"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:7A1G"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 197 AA; 22443 MW; A5A3641D4D7A34F5 CRC64;
MPRAPRTYSK TYSTPKRPYE SSRLDAELKL AGEFGLKNKK EIYRISFQLS KIRRAARDLL
TRDEKDPKRL FEGNALIRRL VRVGVLSEDK KKLDYVLALK VEDFLERRLQ TQVYKLGLAK
SVHHARVLIT QRHIAVGKQI VNIPSFMVRL DSEKHIDFAP TSPFGGARPG RVARRNAARK
AEASGEAADE ADEADEE
