ID RL9A_YEAST Reviewed; 191 AA. AC P05738; D6VU02; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 2. DT 04-NOV-2026, entry version 224. DE RecName: Full=Large ribosomal subunit protein uL6A {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L9-A {ECO:0000303|PubMed:9559554}; DE AltName: Full=L8; DE AltName: Full=RP24; DE AltName: Full=YL11; GN Name=RPL9A {ECO:0000303|PubMed:9559554}; Synonyms=RPL8A, RPL9; GN OrderedLocusNames=YGL147C; 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=1945856; DOI=10.1093/nar/19.20.5785; RA Jones D.G.L., Reusser U., Braus G.H.; RT "Cloning and characterisation of a yeast homolog of the mammalian ribosomal RT protein L9."; RL Nucleic Acids Res. 19:5785-5785(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=9046099; RX DOI=10.1002/(sici)1097-0061(199702)13:2<177::aid-yea62>3.0.co;2-2; RA Voet M., Defoor E., Verhasselt P., Riles L., Robben J., Volckaert G.; RT "The sequence of a nearly unclonable 22.8 kb segment on the left arm RT chromosome VII from Saccharomyces cerevisiae reveals ARO2, RPL9A, TIP1, RT MRF1 genes and six new open reading frames."; RL Yeast 13:177-182(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; DOI=10.1038/387s081; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(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 PARTIAL PROTEIN SEQUENCE OF 1-40. RX PubMed=18782943; DOI=10.1007/bf00341461; RA Otaka E., Higo K., Itoh T.; RT "Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence RT characterization of twenty-four proteins from cytoplasmic ribosomes."; RL Mol. Gen. Genet. 195:544-546(1984). RN [6] 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 [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 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 7-184, 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 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 OF 80S RIBOSOME, SUBUNIT, AND 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). uL6 lines the binding pocket for CC eukaryotic elongation factor 2 (eEF2) (PubMed:22096102, CC PubMed:9559554). {ECO:0000269|PubMed:22096102, CC ECO:0000305|PubMed:9559554}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:22096102}. CC -!- MISCELLANEOUS: Present with 52400 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- MISCELLANEOUS: There are 2 genes for uL6 in yeast. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 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; X60190; CAA42746.1; -; Genomic_DNA. DR EMBL; X99960; CAA68215.1; -; Genomic_DNA. DR EMBL; Z72669; CAA96859.1; -; Genomic_DNA. DR EMBL; BK006941; DAA07963.1; -; Genomic_DNA. DR PIR; S19077; R5BYL9. DR RefSeq; NP_011368.3; NM_001181012.3. DR PDB; 3J16; EM; -; F=1-191. DR PDB; 3J6X; EM; 6.10 A; L9=1-191. DR PDB; 3J6Y; EM; 6.10 A; L9=1-191. DR PDB; 3J77; EM; 6.20 A; L9=1-191. DR PDB; 3J78; EM; 6.30 A; L9=1-191. DR PDB; 3JCT; EM; 3.08 A; H=1-191. DR PDB; 4U3M; X-ray; 3.00 A; L9/l9=1-191. DR PDB; 4U3N; X-ray; 3.20 A; L9/l9=1-191. DR PDB; 4U3U; X-ray; 2.90 A; L9/l9=1-191. DR PDB; 4U4N; X-ray; 3.10 A; L9/l9=1-191. DR PDB; 4U4O; X-ray; 3.60 A; L9/l9=1-191. DR PDB; 4U4Q; X-ray; 3.00 A; L9/l9=1-191. DR PDB; 4U4R; X-ray; 2.80 A; L9/l9=1-191. DR PDB; 4U4U; X-ray; 3.00 A; L9/l9=1-191. DR PDB; 4U4Y; X-ray; 3.20 A; L9/l9=1-191. DR PDB; 4U4Z; X-ray; 3.10 A; L9/l9=1-191. DR PDB; 4U50; X-ray; 3.20 A; L9/l9=1-191. DR PDB; 4U51; X-ray; 3.20 A; L9/l9=1-191. DR PDB; 4U52; X-ray; 3.00 A; L9/l9=1-191. DR PDB; 4U53; X-ray; 3.30 A; L9/l9=1-191. DR PDB; 4U55; X-ray; 3.20 A; L9/l9=1-191. DR PDB; 4U56; X-ray; 3.45 A; L9/l9=1-191. DR PDB; 4U6F; X-ray; 3.10 A; L9/l9=1-191. DR PDB; 4V4B; EM; 11.70 A; BH=1-191. DR PDB; 4V5Z; EM; 8.70 A; Be=1-189. DR PDB; 4V6I; EM; 8.80 A; BF=1-191. DR PDB; 4V7F; EM; 8.70 A; F=1-191. DR PDB; 4V7R; X-ray; 4.00 A; BI/DI=1-191. DR PDB; 4V88; X-ray; 3.00 A; BH/DH=1-191. DR PDB; 4V8T; EM; 8.10 A; H=1-191. DR PDB; 4V8Y; EM; 4.30 A; BH=1-191. DR PDB; 4V8Z; EM; 6.60 A; BH=1-191. DR PDB; 4V91; EM; 3.70 A; H=1-191. DR PDB; 5APN; EM; 3.91 A; H=1-191. DR PDB; 5APO; EM; 3.41 A; H=1-191. DR PDB; 5DAT; X-ray; 3.15 A; L9/l9=1-191. DR PDB; 5DC3; X-ray; 3.25 A; L9/l9=1-191. DR PDB; 5DGE; X-ray; 3.45 A; L9/l9=1-191. DR PDB; 5DGF; X-ray; 3.30 A; L9/l9=1-191. DR PDB; 5DGV; X-ray; 3.10 A; L9/l9=1-191. DR PDB; 5FCI; X-ray; 3.40 A; L9/l9=1-191. DR PDB; 5FCJ; X-ray; 3.10 A; L9/l9=1-191. DR PDB; 5GAK; EM; 3.88 A; L=1-191. DR PDB; 5H4P; EM; 3.07 A; H=1-191. DR PDB; 5I4L; X-ray; 3.10 A; L9/l9=1-191. DR PDB; 5JCS; EM; 9.50 A; H=1-191. DR PDB; 5JUO; EM; 4.00 A; M=1-191. DR PDB; 5JUP; EM; 3.50 A; M=1-191. DR PDB; 5JUS; EM; 4.20 A; M=1-191. DR PDB; 5JUT; EM; 4.00 A; M=1-191. DR PDB; 5JUU; EM; 4.00 A; M=1-191. DR PDB; 5LYB; X-ray; 3.25 A; L9/l9=1-191. DR PDB; 5M1J; EM; 3.30 A; H5=1-191. DR PDB; 5MC6; EM; 3.80 A; AD=1-191. DR PDB; 5MEI; X-ray; 3.50 A; CK/q=1-191. DR PDB; 5NDG; X-ray; 3.70 A; L9/l9=1-191. DR PDB; 5NDV; X-ray; 3.30 A; L9/l9=1-191. DR PDB; 5NDW; X-ray; 3.70 A; L9/l9=1-191. DR PDB; 5OBM; X-ray; 3.40 A; L9/l9=1-191. DR PDB; 5ON6; X-ray; 3.10 A; CK/q=1-191. DR PDB; 5T62; EM; 3.30 A; K=1-191. DR PDB; 5T6R; EM; 4.50 A; K=1-191. DR PDB; 5TBW; X-ray; 3.00 A; CK/q=1-191. DR PDB; 5TGA; X-ray; 3.30 A; L9/l9=1-191. DR PDB; 5TGM; X-ray; 3.50 A; L9/l9=1-191. DR PDB; 5Z3G; EM; 3.65 A; L=1-191. DR PDB; 6ELZ; EM; 3.30 A; H=1-191. DR PDB; 6EM1; EM; 3.60 A; H=1-191. DR PDB; 6EM5; EM; 4.30 A; H=1-191. DR PDB; 6FT6; EM; 3.90 A; H=1-191. DR PDB; 6GQ1; EM; 4.40 A; H=1-191. DR PDB; 6GQB; EM; 3.90 A; H=1-191. DR PDB; 6GQV; EM; 4.00 A; H=1-191. DR PDB; 6HD7; EM; 3.40 A; L=1-191. DR PDB; 6HHQ; X-ray; 3.10 A; CK/q=1-191. DR PDB; 6I7O; EM; 5.30 A; AD/XD=1-190. DR PDB; 6M62; EM; 3.20 A; H=1-191. DR PDB; 6N8J; EM; 3.50 A; H=1-191. DR PDB; 6N8K; EM; 3.60 A; H=1-191. DR PDB; 6N8L; EM; 3.60 A; H=1-191. DR PDB; 6N8M; EM; 3.50 A; K=1-191. DR PDB; 6N8N; EM; 3.80 A; K=1-191. DR PDB; 6N8O; EM; 3.50 A; K=1-191. DR PDB; 6OIG; EM; 3.80 A; H=1-191. DR PDB; 6Q8Y; EM; 3.10 A; AD=1-191. DR PDB; 6QIK; EM; 3.10 A; F=1-191. DR PDB; 6QT0; EM; 3.40 A; F=1-189. DR PDB; 6QTZ; EM; 3.50 A; F=1-191. DR PDB; 6R84; EM; 3.60 A; 7=1-191. DR PDB; 6R86; EM; 3.40 A; 7=1-191. DR PDB; 6R87; EM; 3.40 A; 7=1-191. DR PDB; 6RI5; EM; 3.30 A; F=1-191. DR PDB; 6RZZ; EM; 3.20 A; F=1-191. DR PDB; 6S05; EM; 3.90 A; F=1-191. DR PDB; 6S47; EM; 3.28 A; AK=1-191. DR PDB; 6SNT; EM; 2.80 A; o=1-191. DR PDB; 6SV4; EM; 3.30 A; AD/XD/zD=1-190. DR PDB; 6T4Q; EM; 2.60 A; LH=1-191. DR PDB; 6T7I; EM; 3.20 A; LH=1-191. DR PDB; 6T7T; EM; 3.10 A; LH=1-191. DR PDB; 6T83; EM; 4.00 A; Hy/Ka=1-191. DR PDB; 6TB3; EM; 2.80 A; AD=1-191. DR PDB; 6TNU; EM; 3.10 A; AD=1-191. DR PDB; 6YLG; EM; 3.00 A; H=1-191. DR PDB; 6YLH; EM; 3.10 A; H=1-191. DR PDB; 6YLX; EM; 3.90 A; H=1-191. DR PDB; 6YLY; EM; 3.80 A; H=1-191. DR PDB; 6Z6J; EM; 3.40 A; LH=1-191. DR PDB; 6Z6K; EM; 3.40 A; LH=1-191. DR PDB; 7AZY; EM; 2.88 A; e=1-191. DR PDB; 7B7D; EM; 3.30 A; LK=1-191. DR PDB; 7BT6; EM; 3.12 A; H=1-191. DR PDB; 7BTB; EM; 3.22 A; H=1-191. DR PDB; 7MPI; EM; 3.05 A; AH=1-190. DR PDB; 7MPJ; EM; 2.70 A; AH=1-190. DR PDB; 7N8B; EM; 3.05 A; AH=1-190. DR PDB; 7NAC; EM; 3.04 A; H=1-191. DR PDB; 7NRC; EM; 3.90 A; LK=1-191. DR PDB; 7NRD; EM; 4.36 A; LK=1-191. DR PDB; 7OF1; EM; 3.10 A; H=1-191. DR PDB; 7OH3; EM; 3.40 A; H=1-191. DR PDB; 7OHP; EM; 3.90 A; H=1-191. DR PDB; 7OHQ; EM; 3.10 A; H=1-191. DR PDB; 7OHR; EM; 4.72 A; H=1-191. DR PDB; 7OHS; EM; 4.38 A; H=1-191. DR PDB; 7OHT; EM; 4.70 A; H=1-191. DR PDB; 7OHU; EM; 3.70 A; H=1-191. DR PDB; 7OHV; EM; 3.90 A; H=1-191. DR PDB; 7OHW; EM; 3.50 A; H=1-191. DR PDB; 7OHX; EM; 3.30 A; H=1-191. DR PDB; 7OHY; EM; 3.90 A; H=1-191. DR PDB; 7OSA; X-ray; 3.00 A; uL6=1-191. DR PDB; 7OSM; X-ray; 3.00 A; uL6=1-191. DR PDB; 7R7A; EM; 3.04 A; H=1-191. DR PDB; 7RR5; EM; 3.23 A; LH=1-191. DR PDB; 7TOO; EM; 2.70 A; AL09=1-191. DR PDB; 7TOP; EM; 2.40 A; AL09=1-191. DR PDB; 7U0H; EM; 2.76 A; H=1-191. DR PDB; 7UG6; EM; 2.90 A; H=1-191. DR PDB; 7UOO; EM; 2.34 A; H=1-191. DR PDB; 7UQB; EM; 2.43 A; H=1-191. DR PDB; 7UQZ; EM; 2.44 A; H=1-191. DR PDB; 7V08; EM; 2.36 A; H=1-191. DR PDB; 7Z34; EM; 3.80 A; H=1-191. DR PDB; 7ZPQ; EM; 3.47 A; BH=1-191. DR PDB; 7ZRS; EM; 4.80 A; BH=1-191. DR PDB; 7ZS5; EM; 3.20 A; BJ=1-191. DR PDB; 7ZUW; EM; 4.30 A; BH=1-191. DR PDB; 7ZUX; EM; 2.50 A; EH=1-191. DR PDB; 7ZW0; EM; 2.40 A; LL=1-191. DR PDB; 8AAF; EM; 2.50 A; q=1-191. DR PDB; 8AGT; EM; 2.60 A; q=1-191. DR PDB; 8AGU; EM; 2.70 A; q=1-191. DR PDB; 8AGV; EM; 2.60 A; q=1-191. DR PDB; 8AGW; EM; 2.60 A; q=1-191. DR PDB; 8AGX; EM; 2.40 A; q=1-191. DR PDB; 8AGZ; EM; 2.60 A; q=1-191. DR PDB; 8BIP; EM; 3.10 A; LH=1-191. DR PDB; 8BJQ; EM; 3.80 A; LH=1-191. DR PDB; 8BN3; EM; 2.40 A; L9=1-189. DR PDB; 8BQD; EM; 3.90 A; AD=1-191. DR PDB; 8BQX; EM; 3.80 A; AD=1-191. DR PDB; 8CCS; EM; 1.97 A; LL=1-191. DR PDB; 8CDL; EM; 2.72 A; LL=1-191. DR PDB; 8CDR; EM; 2.04 A; LL=1-191. DR PDB; 8CKU; EM; 3.11 A; LL=1-191. DR PDB; 8EUB; EM; 2.52 A; AH=1-191. DR PDB; 8EVP; EM; 2.38 A; AH=1-191. DR PDB; 8EVQ; EM; 2.72 A; AH=1-191. DR PDB; 8EVR; EM; 2.87 A; AH=1-191. DR PDB; 8EVS; EM; 2.62 A; AH=1-191. DR PDB; 8EVT; EM; 2.20 A; AH=1-191. DR PDB; 8EWB; EM; 2.87 A; AH=1-191. DR PDB; 8EWC; EM; 2.45 A; AH=1-191. DR PDB; 8HFR; EM; 2.64 A; Ib=1-191. DR PDB; 8K2D; EM; 3.20 A; LH=1-191. DR PDB; 8K82; EM; 3.00 A; LH=1-191. DR PDB; 8P4V; X-ray; 3.16 A; CK/q=1-191. DR PDB; 8P85; X-ray; 2.90 A; CK/q=1-191. DR PDB; 8P8M; EM; 2.66 A; LM=1-191. DR PDB; 8P8N; EM; 2.15 A; LM=1-191. DR PDB; 8P8U; EM; 2.23 A; LM=1-191. DR PDB; 8P9A; X-ray; 2.90 A; CK/q=1-191. DR PDB; 8PFR; EM; 2.15 A; LM=1-191. DR PDB; 8PNN; X-ray; 2.90 A; CK/q=1-191. DR PDB; 8T2X; EM; 2.46 A; AH=1-191. DR PDB; 8T2Y; EM; 2.20 A; AH=1-191. DR PDB; 8T2Z; EM; 2.40 A; AH=1-191. DR PDB; 8T30; EM; 2.88 A; AH=1-191. DR PDB; 8T3A; EM; 2.86 A; AH=1-191. DR PDB; 8T3B; EM; 3.08 A; AH=1-191. DR PDB; 8T3C; EM; 3.86 A; AH=1-191. DR PDB; 8T3D; EM; 2.95 A; AH=1-191. DR PDB; 8T3E; EM; 3.04 A; AH=1-191. DR PDB; 8T3F; EM; 3.09 A; AH=1-191. DR PDB; 8UT0; EM; 3.22 A; LK=1-191. DR PDB; 8UTI; EM; 3.13 A; LK=1-191. DR PDB; 8V83; EM; 2.53 A; H=1-191. DR PDB; 8V84; EM; 2.70 A; H=1-191. DR PDB; 8V87; EM; 2.66 A; H=1-191. DR PDB; 8XU8; EM; 3.40 A; K=1-191. DR PDB; 8Y0U; EM; 3.59 A; LH=1-191. DR PDB; 8YLD; EM; 3.90 A; K=1-191. DR PDB; 8YLR; EM; 3.90 A; K=1-191. DR PDB; 8Z70; EM; 3.20 A; K=1-191. DR PDB; 8Z71; EM; 3.60 A; K=1-191. DR PDB; 8ZGR; EM; 2.70 A; LK=1-191. DR PDB; 8ZGY; EM; 2.80 A; LK=1-191. DR PDB; 8ZH3; EM; 2.70 A; LK=1-191. DR PDB; 8ZHB; EM; 2.60 A; LK=1-191. DR PDB; 8ZHC; EM; 2.30 A; LK=1-191. DR PDB; 9DOV; EM; 2.49 A; AH=1-191. DR PDB; 9DP7; EM; 2.38 A; AH=1-191. DR PDB; 9F58; EM; 3.10 A; i=1-191. DR PDB; 9F9S; EM; 2.90 A; LD/MD=1-191. DR PDB; 9OFV; EM; 3.16 A; q=1-191. DR PDB; 9PN5; EM; 1.75 A; AH=1-191. DR PDB; 9R9O; EM; 2.90 A; LH=1-191. DR PDB; 9R9P; EM; 3.00 A; LH=1-191. DR AlphaFoldDB; P05738; -. DR EMDB; EMD-0047; -. DR EMDB; EMD-0048; -. DR EMDB; EMD-0049; -. DR EMDB; EMD-0202; -. DR EMDB; EMD-0369; -. DR EMDB; EMD-0370; -. DR EMDB; EMD-0371; -. DR EMDB; EMD-0372; -. DR EMDB; EMD-0373; -. DR EMDB; EMD-0374; -. DR EMDB; EMD-10068; -. DR EMDB; EMD-10071; -. DR EMDB; EMD-10098; -. DR EMDB; EMD-10262; -. DR EMDB; EMD-10315; -. DR EMDB; EMD-10377; -. DR EMDB; EMD-10396; -. DR EMDB; EMD-10397; -. DR EMDB; EMD-10398; -. DR EMDB; EMD-10431; -. DR EMDB; EMD-10537; -. DR EMDB; EMD-10838; -. DR EMDB; EMD-10839; -. DR EMDB; EMD-10841; -. DR EMDB; EMD-10842; -. DR EMDB; EMD-11096; -. DR EMDB; EMD-11097; -. DR EMDB; EMD-11951; -. DR EMDB; EMD-12081; -. DR EMDB; EMD-12534; -. DR EMDB; EMD-12535; -. DR EMDB; EMD-12866; -. DR EMDB; EMD-12892; -. DR EMDB; EMD-12904; -. DR EMDB; EMD-12905; -. DR EMDB; EMD-12906; -. DR EMDB; EMD-12907; -. DR EMDB; EMD-12908; -. DR EMDB; EMD-12909; -. DR EMDB; EMD-12910; -. DR EMDB; EMD-12911; -. DR EMDB; EMD-12912; -. DR EMDB; EMD-12913; -. DR EMDB; EMD-14471; -. DR EMDB; EMD-14861; -. DR EMDB; EMD-14921; -. DR EMDB; EMD-14926; -. DR EMDB; EMD-14979; -. DR EMDB; EMD-14990; -. DR EMDB; EMD-15296; -. DR EMDB; EMD-15423; -. DR EMDB; EMD-15424; -. DR EMDB; EMD-15425; -. DR EMDB; EMD-15426; -. DR EMDB; EMD-15427; -. DR EMDB; EMD-15428; -. DR EMDB; EMD-16086; -. DR EMDB; EMD-16090; -. DR EMDB; EMD-16191; -. DR EMDB; EMD-16563; -. DR EMDB; EMD-16591; -. DR EMDB; EMD-16594; -. DR EMDB; EMD-16702; -. DR EMDB; EMD-17549; -. DR EMDB; EMD-17550; -. DR EMDB; EMD-17552; -. DR EMDB; EMD-17653; -. DR EMDB; EMD-20077; -. DR EMDB; EMD-23934; -. DR EMDB; EMD-23935; -. DR EMDB; EMD-24235; -. DR EMDB; EMD-24269; -. DR EMDB; EMD-24296; -. DR EMDB; EMD-24652; -. DR EMDB; EMD-26033; -. DR EMDB; EMD-26034; -. DR EMDB; EMD-26259; -. DR EMDB; EMD-26485; -. DR EMDB; EMD-26651; -. DR EMDB; EMD-26686; -. DR EMDB; EMD-26703; -. DR EMDB; EMD-26941; -. DR EMDB; EMD-28610; -. DR EMDB; EMD-28632; -. DR EMDB; EMD-28633; -. DR EMDB; EMD-28634; -. DR EMDB; EMD-28635; -. DR EMDB; EMD-28636; -. DR EMDB; EMD-28642; -. DR EMDB; EMD-28643; -. DR EMDB; EMD-30108; -. DR EMDB; EMD-30170; -. DR EMDB; EMD-30174; -. DR EMDB; EMD-3461; -. DR EMDB; EMD-34725; -. DR EMDB; EMD-36839; -. DR EMDB; EMD-36945; -. DR EMDB; EMD-38660; -. DR EMDB; EMD-40990; -. DR EMDB; EMD-40991; -. DR EMDB; EMD-40992; -. DR EMDB; EMD-40993; -. DR EMDB; EMD-40997; -. DR EMDB; EMD-40998; -. DR EMDB; EMD-40999; -. DR EMDB; EMD-41000; -. DR EMDB; EMD-41001; -. DR EMDB; EMD-41002; -. DR EMDB; EMD-4140; -. DR EMDB; EMD-42525; -. DR EMDB; EMD-42540; -. DR EMDB; EMD-43017; -. DR EMDB; EMD-4302; -. DR EMDB; EMD-43021; -. DR EMDB; EMD-43027; -. DR EMDB; EMD-4427; -. DR EMDB; EMD-4474; -. DR EMDB; EMD-4560; -. DR EMDB; EMD-4630; -. DR EMDB; EMD-4636; -. DR EMDB; EMD-47093; -. DR EMDB; EMD-47098; -. DR EMDB; EMD-4751; -. DR EMDB; EMD-4752; -. DR EMDB; EMD-4753; -. DR EMDB; EMD-4884; -. DR EMDB; EMD-50188; -. DR EMDB; EMD-50259; -. DR EMDB; EMD-53860; -. DR EMDB; EMD-53861; -. DR EMDB; EMD-60088; -. DR EMDB; EMD-60091; -. DR EMDB; EMD-60094; -. DR EMDB; EMD-60097; -. DR EMDB; EMD-60098; -. DR EMDB; EMD-6878; -. DR EMDB; EMD-70444; -. DR EMDB; EMD-71745; -. DR EMDB; EMD-8362; -. DR EMDB; EMD-8368; -. DR SMR; P05738; -. DR BioGRID; 33105; 371. DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit. DR DIP; DIP-4826N; -. DR FunCoup; P05738; 1137. DR IntAct; P05738; 117. DR STRING; 4932.YGL147C; -. DR iPTMnet; P05738; -. DR PaxDb; 4932-YGL147C; -. DR PeptideAtlas; P05738; -. DR EnsemblFungi; YGL147C_mRNA; YGL147C; YGL147C. DR GeneID; 852730; -. DR KEGG; sce:YGL147C; -. DR AGR; SGD:S000003115; -. DR SGD; S000003115; RPL9A. DR VEuPathDB; FungiDB:YGL147C; -. DR eggNOG; KOG3255; Eukaryota. DR HOGENOM; CLU_065464_0_0_1; -. DR InParanoid; P05738; -. DR OMA; ADIHQIC; -. DR OrthoDB; 10252633at2759; -. DR BioCyc; YEAST:G3O-30641-MONOMER; -. DR BioGRID-ORCS; 852730; 2 hits in 10 CRISPR screens. DR EvolutionaryTrace; P05738; -. DR PRO; PR:P05738; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P05738; protein. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD. DR GO; GO:0019843; F:rRNA binding; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD. DR GO; GO:0002181; P:cytoplasmic translation; IDA:SGD. DR FunFam; 3.90.930.12:FF:000003; 60S ribosomal protein L9; 1. DR FunFam; 3.90.930.12:FF:000004; 60S ribosomal protein L9; 1. DR Gene3D; 3.90.930.12; Ribosomal protein L6, alpha-beta domain; 2. DR InterPro; IPR000702; Ribosomal_uL6-like. DR InterPro; IPR036789; Ribosomal_uL6-like_a/b-dom_sf. DR InterPro; IPR020040; Ribosomal_uL6_a/b-dom. DR InterPro; IPR002359; Ribosomal_uL6_CS2. DR PANTHER; PTHR11655:SF16; 60S RIBOSOMAL PROTEIN L9; 1. DR PANTHER; PTHR11655; 60S/50S RIBOSOMAL PROTEIN L6/L9; 1. DR Pfam; PF00347; Ribosomal_L6; 2. DR PIRSF; PIRSF002162; Ribosomal_L6; 1. DR SUPFAM; SSF56053; Ribosomal protein L6; 2. DR PROSITE; PS00700; RIBOSOMAL_L6_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome; KW Ribonucleoprotein; Ribosomal protein. FT CHAIN 1..191 FT /note="Large ribosomal subunit protein uL6A" FT /id="PRO_0000131111" FT STRAND 3..11 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 17..28 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 33..37 FT /evidence="ECO:0007829|PDB:8CCS" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:8CDR" FT STRAND 44..60 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 62..83 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 86..93 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 100..104 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 111..115 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:5TGA" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:8PFR" FT STRAND 143..149 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 151..164 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:8T3D" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 178..185 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 187..189 FT /evidence="ECO:0007829|PDB:8CDR" SQ SEQUENCE 191 AA; 21569 MW; CAA342FCDD061175 CRC64; MKYIQTEQQI EVPEGVTVSI KSRIVKVVGP RGTLTKNLKH IDVTFTKVNN QLIKVAVHNG GRKHVAALRT VKSLVDNMIT GVTKGYKYKM RYVYAHFPIN VNIVEKDGAK FIEVRNFLGD KKIRNVPVRD GVTIEFSTNV KDEIVLSGNS VEDVSQNAAD LQQICRVRNK DIRKFLDGIY VSHKGFITED L //