RL43A_YEAST
ID RL43A_YEAST Reviewed; 92 AA.
AC P0CX25; D6VWR3; P49631;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=60S ribosomal protein L43-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L37a;
DE AltName: Full=Large ribosomal subunit protein eL43-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YL35;
GN Name=RPL43A {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YPR043W;
GN ORFNames=YP9499.02;
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 46191 / IL125-2B;
RX PubMed=9730282;
RX DOI=10.1002/(sici)1097-0061(199808)14:11<1027::aid-yea295>3.0.co;2-s;
RA Waskiewicz-Staniorowska B., Skala J., Jasinski M., Grenson M., Goffeau A.,
RA Ulaszewski S.;
RT "Functional analysis of three adjacent open reading frames from the right
RT arm of yeast chromosome XVI.";
RL Yeast 14:1027-1039(1998).
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 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 MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=11983894; DOI=10.1073/pnas.082119899;
RA Lee S.-W., Berger S.J., Martinovic S., Pasa-Tolic L., Anderson G.A.,
RA Shen Y., Zhao R., Smith R.D.;
RT "Direct mass spectrometric analysis of intact proteins of the yeast large
RT ribosomal subunit using capillary LC/FTICR.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5942-5947(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
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 10-82, 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, 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 (4.0 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 (3.0 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. {ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU). 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 -!- MASS SPECTROMETRY: Mass=9953.311; Method=Electrospray;
CC Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:11983894};
CC -!- MISCELLANEOUS: Present with 44600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eL43 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL43 family.
CC {ECO:0000305}.
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DR EMBL; Z73616; CAA97993.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94991.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89164.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11468.1; -; Genomic_DNA.
DR PIR; S54068; S54068.
DR RefSeq; NP_012628.3; NM_001181752.3.
DR RefSeq; NP_015368.1; NM_001184140.1.
DR PDB; 3J6X; EM; 6.10 A; 83=1-92.
DR PDB; 3J6Y; EM; 6.10 A; 83=1-92.
DR PDB; 3J77; EM; 6.20 A; 93=1-92.
DR PDB; 3J78; EM; 6.30 A; 93=1-92.
DR PDB; 3JCT; EM; 3.08 A; p=1-92.
DR PDB; 4U3M; X-ray; 3.00 A; Q3/q3=2-92.
DR PDB; 4U3N; X-ray; 3.20 A; Q3/q3=2-92.
DR PDB; 4U3U; X-ray; 2.90 A; Q3/q3=2-92.
DR PDB; 4U4N; X-ray; 3.10 A; Q3/q3=2-92.
DR PDB; 4U4O; X-ray; 3.60 A; Q3/q3=2-92.
DR PDB; 4U4Q; X-ray; 3.00 A; Q3/q3=2-92.
DR PDB; 4U4R; X-ray; 2.80 A; Q3/q3=2-92.
DR PDB; 4U4U; X-ray; 3.00 A; Q3/q3=2-92.
DR PDB; 4U4Y; X-ray; 3.20 A; Q3/q3=2-92.
DR PDB; 4U4Z; X-ray; 3.10 A; Q3/q3=2-92.
DR PDB; 4U50; X-ray; 3.20 A; Q3/q3=2-92.
DR PDB; 4U51; X-ray; 3.20 A; Q3/q3=2-92.
DR PDB; 4U52; X-ray; 3.00 A; Q3/q3=2-92.
DR PDB; 4U53; X-ray; 3.30 A; Q3/q3=2-92.
DR PDB; 4U55; X-ray; 3.20 A; Q3/q3=2-92.
DR PDB; 4U56; X-ray; 3.45 A; Q3/q3=2-92.
DR PDB; 4U6F; X-ray; 3.10 A; Q3/q3=2-92.
DR PDB; 4V4B; EM; 11.70 A; B9=2-92.
DR PDB; 4V6I; EM; 8.80 A; Bm=1-92.
DR PDB; 4V7F; EM; 8.70 A; k=1-92.
DR PDB; 4V7R; X-ray; 4.00 A; Bg/Dg=1-92.
DR PDB; 4V88; X-ray; 3.00 A; Bp/Dp=1-92.
DR PDB; 4V8T; EM; 8.10 A; p=1-92.
DR PDB; 4V91; EM; 3.70 A; p=1-92.
DR PDB; 5APN; EM; 3.91 A; p=1-92.
DR PDB; 5APO; EM; 3.41 A; p=1-92.
DR PDB; 5DAT; X-ray; 3.15 A; Q3/q3=2-92.
DR PDB; 5DC3; X-ray; 3.25 A; Q3/q3=2-92.
DR PDB; 5DGE; X-ray; 3.45 A; Q3/q3=2-92.
DR PDB; 5DGF; X-ray; 3.30 A; Q3/q3=2-92.
DR PDB; 5DGV; X-ray; 3.10 A; Q3/q3=2-92.
DR PDB; 5FCI; X-ray; 3.40 A; Q3/q3=2-92.
DR PDB; 5FCJ; X-ray; 3.10 A; Q3/q3=2-92.
DR PDB; 5FL8; EM; 9.50 A; p=1-92.
DR PDB; 5GAK; EM; 3.88 A; D=1-92.
DR PDB; 5H4P; EM; 3.07 A; p=1-92.
DR PDB; 5I4L; X-ray; 3.10 A; Q3/q3=2-92.
DR PDB; 5JCS; EM; 9.50 A; p=1-92.
DR PDB; 5JUO; EM; 4.00 A; UA=1-92.
DR PDB; 5JUP; EM; 3.50 A; UA=1-92.
DR PDB; 5JUS; EM; 4.20 A; UA=1-92.
DR PDB; 5JUT; EM; 4.00 A; UA=1-92.
DR PDB; 5JUU; EM; 4.00 A; UA=1-92.
DR PDB; 5LYB; X-ray; 3.25 A; Q3/q3=2-92.
DR PDB; 5MC6; EM; 3.80 A; AT=1-92.
DR PDB; 5MEI; X-ray; 3.50 A; AQ/DR=2-92.
DR PDB; 5NDG; X-ray; 3.70 A; Q3/q3=2-92.
DR PDB; 5NDV; X-ray; 3.30 A; Q3/q3=2-92.
DR PDB; 5NDW; X-ray; 3.70 A; Q3/q3=2-92.
DR PDB; 5OBM; X-ray; 3.40 A; Q3/q3=2-92.
DR PDB; 5ON6; X-ray; 3.10 A; AQ/DR=2-92.
DR PDB; 5T62; EM; 3.30 A; R=1-92.
DR PDB; 5T6R; EM; 4.50 A; R=1-92.
DR PDB; 5TBW; X-ray; 3.00 A; AQ/DR=2-92.
DR PDB; 5TGA; X-ray; 3.30 A; Q3/q3=2-92.
DR PDB; 5TGM; X-ray; 3.50 A; Q3/q3=2-92.
DR PDB; 6FT6; EM; 3.90 A; p=1-92.
DR PDB; 6GQ1; EM; 4.40 A; p=2-92.
DR PDB; 6GQB; EM; 3.90 A; p=2-92.
DR PDB; 6GQV; EM; 4.00 A; p=2-92.
DR PDB; 6HD7; EM; 3.40 A; D=1-92.
DR PDB; 6HHQ; X-ray; 3.10 A; AQ/DR=1-92.
DR PDB; 6I7O; EM; 5.30 A; AT/XT=2-92.
DR PDB; 6M62; EM; 3.20 A; p=1-92.
DR PDB; 6N8J; EM; 3.50 A; p=1-92.
DR PDB; 6N8K; EM; 3.60 A; p=1-92.
DR PDB; 6N8L; EM; 3.60 A; p=1-92.
DR PDB; 6N8M; EM; 3.50 A; R=1-92.
DR PDB; 6N8N; EM; 3.80 A; R=1-92.
DR PDB; 6N8O; EM; 3.50 A; R=1-92.
DR PDB; 6OIG; EM; 3.80 A; p=2-92.
DR PDB; 6Q8Y; EM; 3.10 A; AT=2-92.
DR PDB; 6QIK; EM; 3.10 A; m=1-92.
DR PDB; 6QT0; EM; 3.40 A; m=1-92.
DR PDB; 6QTZ; EM; 3.50 A; m=1-92.
DR PDB; 6R84; EM; 3.60 A; D=2-92.
DR PDB; 6R86; EM; 3.40 A; D=2-92.
DR PDB; 6R87; EM; 3.40 A; D=2-92.
DR PDB; 6RI5; EM; 3.30 A; m=1-92.
DR PDB; 6RZZ; EM; 3.20 A; m=1-92.
DR PDB; 6S05; EM; 3.90 A; m=1-92.
DR PDB; 6S47; EM; 3.28 A; Ar=2-92.
DR PDB; 6SNT; EM; 2.80 A; aa=1-92.
DR PDB; 6SV4; EM; 3.30 A; AT/XT/zT=1-92.
DR PDB; 6T4Q; EM; 2.60 A; Lp=2-92.
DR PDB; 6T7I; EM; 3.20 A; Lp=1-92.
DR PDB; 6T7T; EM; 3.10 A; Lp=1-92.
DR PDB; 6T83; EM; 4.00 A; aa/pb=1-92.
DR PDB; 6TB3; EM; 2.80 A; AT=2-92.
DR PDB; 6TNU; EM; 3.10 A; AT=2-92.
DR PDB; 6WOO; EM; 2.90 A; p=3-89.
DR PDB; 6XIQ; EM; 4.20 A; p=1-92.
DR PDB; 6XIR; EM; 3.20 A; p=1-92.
DR PDB; 6YLG; EM; 3.00 A; p=1-92.
DR PDB; 6YLH; EM; 3.10 A; p=1-92.
DR PDB; 6YLY; EM; 3.80 A; p=1-92.
DR PDB; 6Z6J; EM; 3.40 A; Lp=1-92.
DR PDB; 6Z6K; EM; 3.40 A; Lp=1-92.
DR PDB; 7AZY; EM; 2.88 A; U=1-92.
DR PDB; 7B7D; EM; 3.30 A; Ll=2-92.
DR PDB; 7BT6; EM; 3.12 A; p=1-92.
DR PDB; 7BTB; EM; 3.22 A; p=1-92.
DR PDB; 7NRC; EM; 3.90 A; Lr=2-92.
DR PDB; 7NRD; EM; 4.36 A; Lr=2-92.
DR PDB; 7OF1; EM; 3.10 A; p=1-92.
DR PDB; 7OH3; EM; 3.40 A; p=1-92.
DR PDB; 7OHQ; EM; 3.10 A; p=1-92.
DR PDB; 7OSA; X-ray; 3.00 A; eL43=1-92.
DR PDB; 7OSM; X-ray; 3.00 A; eL43=1-92.
DR PDB; 7RR5; EM; 3.23 A; Lp=1-92.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 3JCT; -.
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; 4V7F; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8T; -.
DR PDBsum; 4V91; -.
DR PDBsum; 5APN; -.
DR PDBsum; 5APO; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5FL8; -.
DR PDBsum; 5GAK; -.
DR PDBsum; 5H4P; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JCS; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5T62; -.
DR PDBsum; 5T6R; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HD7; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6N8J; -.
DR PDBsum; 6N8K; -.
DR PDBsum; 6N8L; -.
DR PDBsum; 6N8M; -.
DR PDBsum; 6N8N; -.
DR PDBsum; 6N8O; -.
DR PDBsum; 6OIG; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6QIK; -.
DR PDBsum; 6QT0; -.
DR PDBsum; 6QTZ; -.
DR PDBsum; 6R84; -.
DR PDBsum; 6R86; -.
DR PDBsum; 6R87; -.
DR PDBsum; 6RI5; -.
DR PDBsum; 6RZZ; -.
DR PDBsum; 6S05; -.
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; 6WOO; -.
DR PDBsum; 6XIQ; -.
DR PDBsum; 6XIR; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 7AZY; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OSA; -.
DR PDBsum; 7OSM; -.
DR PDBsum; 7RR5; -.
DR AlphaFoldDB; P0CX25; -.
DR SMR; P0CX25; -.
DR BioGRID; 33849; 148.
DR BioGRID; 36220; 374.
DR IntAct; P0CX25; 13.
DR MINT; P0CX25; -.
DR STRING; 4932.YJR094W-A; -.
DR iPTMnet; P0CX25; -.
DR MaxQB; P0CX25; -.
DR PaxDb; P0CX25; -.
DR PRIDE; P0CX25; -.
DR EnsemblFungi; YJR094W-A_mRNA; YJR094W-A; YJR094W-A.
DR EnsemblFungi; YPR043W_mRNA; YPR043W; YPR043W.
DR GeneID; 853557; -.
DR GeneID; 856156; -.
DR KEGG; sce:YJR094W-A; -.
DR KEGG; sce:YPR043W; -.
DR SGD; S000006247; RPL43A.
DR VEuPathDB; FungiDB:YJR094W-A; -.
DR VEuPathDB; FungiDB:YPR043W; -.
DR eggNOG; KOG0402; Eukaryota.
DR HOGENOM; CLU_141199_1_0_1; -.
DR InParanoid; P0CX25; -.
DR OMA; ISTGIWQ; -.
DR BioCyc; YEAST:G3O-34199-MON; -.
DR EvolutionaryTrace; P0CX25; -.
DR PRO; PR:P0CX25; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P0CX25; protein.
DR ExpressionAtlas; P0CX25; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IC:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR Gene3D; 2.20.25.30; -; 1.
DR HAMAP; MF_00327; Ribosomal_L37Ae; 1.
DR InterPro; IPR002674; Ribosomal_L37ae.
DR InterPro; IPR011331; Ribosomal_L37ae/L37e.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR Pfam; PF01780; Ribosomal_L37ae; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR TIGRFAMs; TIGR00280; eL43_euk_arch; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11983894"
FT CHAIN 2..92
FT /note="60S ribosomal protein L43-A"
FT /id="PRO_0000139838"
FT ZN_FING 39..60
FT /note="C4-type"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 74..91
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 92 AA; 10091 MW; E2057BF56B131730 CRC64;
MAKRTKKVGI TGKYGVRYGS SLRRQVKKLE IQQHARYDCS FCGKKTVKRG AAGIWTCSCC
KKTVAGGAYT VSTAAAATVR STIRRLREMV EA
