RL9A_YEAST
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 03-AUG-2022, entry version 204.
DE RecName: Full=60S ribosomal protein L9-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L8;
DE AltName: Full=Large ribosomal subunit protein uL6-A {ECO:0000303|PubMed:24524803};
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;
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 (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). uL6 lines the binding pocket for
CC eukaryotic elongation factor 2 (eEF2) (PubMed:9559554,
CC PubMed:22096102). {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; 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; 5FL8; EM; 9.50 A; H=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; 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; 7RR5; EM; 3.23 A; LH=1-191.
DR PDBsum; 3J16; -.
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; 4V8Y; -.
DR PDBsum; 4V8Z; -.
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; 5M1J; -.
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; 5Z3G; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM5; -.
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; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6YLX; -.
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; 7OHP; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHT; -.
DR PDBsum; 7OHU; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR PDBsum; 7OHY; -.
DR PDBsum; 7OSA; -.
DR PDBsum; 7OSM; -.
DR PDBsum; 7RR5; -.
DR AlphaFoldDB; P05738; -.
DR SMR; P05738; -.
DR BioGRID; 33105; 250.
DR DIP; DIP-4826N; -.
DR IntAct; P05738; 14.
DR MINT; P05738; -.
DR STRING; 4932.YGL147C; -.
DR iPTMnet; P05738; -.
DR MaxQB; P05738; -.
DR PaxDb; P05738; -.
DR PRIDE; P05738; -.
DR EnsemblFungi; YGL147C_mRNA; YGL147C; YGL147C.
DR GeneID; 852730; -.
DR KEGG; sce:YGL147C; -.
DR SGD; S000003115; RPL9A.
DR VEuPathDB; FungiDB:YGL147C; -.
DR eggNOG; KOG3255; Eukaryota.
DR GeneTree; ENSGT00390000015224; -.
DR HOGENOM; CLU_065464_0_0_1; -.
DR InParanoid; P05738; -.
DR OMA; SARWACH; -.
DR BioCyc; YEAST:G3O-30641-MON; -.
DR EvolutionaryTrace; P05738; -.
DR PRO; PR:P05738; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P05738; protein.
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 Gene3D; 3.90.930.12; -; 2.
DR InterPro; IPR000702; Ribosomal_L6.
DR InterPro; IPR020040; Ribosomal_L6_a/b-dom.
DR InterPro; IPR036789; Ribosomal_L6_a/b-dom_sf.
DR InterPro; IPR002359; Ribosomal_L6_CS2.
DR PANTHER; PTHR11655; PTHR11655; 1.
DR Pfam; PF00347; Ribosomal_L6; 2.
DR PIRSF; PIRSF002162; Ribosomal_L6; 1.
DR SUPFAM; SSF56053; SSF56053; 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="60S ribosomal protein L9-A"
FT /id="PRO_0000131111"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:4U3U"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 62..83
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:4U3M"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 178..189
FT /evidence="ECO:0007829|PDB:4U4R"
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
