RL27A_YEAST
ID RL27A_YEAST Reviewed; 136 AA.
AC P0C2H6; D3DKV5; P38706;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=60S ribosomal protein L27-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=Large ribosomal subunit protein eL27-A {ECO:0000303|PubMed:24524803};
GN Name=RPL27A {ECO:0000303|PubMed:9559554}; Synonyms=RPL27;
GN OrderedLocusNames=YHR010W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
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 [4]
RP CLEAVAGE OF INITIATOR METHIONINE.
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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 -!- MISCELLANEOUS: Present with 7380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eL27 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL27 family.
CC {ECO:0000305}.
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DR EMBL; U10400; AAB68944.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06699.1; -; Genomic_DNA.
DR PIR; S46790; S46790.
DR RefSeq; NP_011874.1; NM_001179140.1.
DR PDB; 3J6X; EM; 6.10 A; 67=1-136.
DR PDB; 3J6Y; EM; 6.10 A; 67=1-136.
DR PDB; 3J77; EM; 6.20 A; 77=1-136.
DR PDB; 3J78; EM; 6.30 A; 77=1-136.
DR PDB; 3JCT; EM; 3.08 A; Z=1-136.
DR PDB; 4U3M; X-ray; 3.00 A; N7/n7=2-136.
DR PDB; 4U3N; X-ray; 3.20 A; N7/n7=2-136.
DR PDB; 4U3U; X-ray; 2.90 A; N7/n7=2-136.
DR PDB; 4U4N; X-ray; 3.10 A; N7/n7=2-136.
DR PDB; 4U4O; X-ray; 3.60 A; N7/n7=2-136.
DR PDB; 4U4Q; X-ray; 3.00 A; N7/n7=2-136.
DR PDB; 4U4R; X-ray; 2.80 A; N7/n7=2-136.
DR PDB; 4U4U; X-ray; 3.00 A; N7/n7=2-136.
DR PDB; 4U4Y; X-ray; 3.20 A; N7/n7=2-136.
DR PDB; 4U4Z; X-ray; 3.10 A; N7/n7=2-136.
DR PDB; 4U50; X-ray; 3.20 A; N7/n7=2-136.
DR PDB; 4U51; X-ray; 3.20 A; N7/n7=2-136.
DR PDB; 4U52; X-ray; 3.00 A; N7/n7=2-136.
DR PDB; 4U53; X-ray; 3.30 A; N7/n7=2-136.
DR PDB; 4U55; X-ray; 3.20 A; N7/n7=2-136.
DR PDB; 4U56; X-ray; 3.45 A; N7/n7=2-136.
DR PDB; 4U6F; X-ray; 3.10 A; N7/n7=2-136.
DR PDB; 4V6I; EM; 8.80 A; Ba=1-136.
DR PDB; 4V7F; EM; 8.70 A; Y=1-136.
DR PDB; 4V88; X-ray; 3.00 A; BZ/DZ=1-136.
DR PDB; 4V8T; EM; 8.10 A; Z=1-136.
DR PDB; 4V8Y; EM; 4.30 A; BZ=2-136.
DR PDB; 4V8Z; EM; 6.60 A; BZ=2-136.
DR PDB; 4V91; EM; 3.70 A; Z=1-136.
DR PDB; 5APN; EM; 3.91 A; Z=1-136.
DR PDB; 5APO; EM; 3.41 A; Z=1-136.
DR PDB; 5DAT; X-ray; 3.15 A; N7/n7=2-136.
DR PDB; 5DC3; X-ray; 3.25 A; N7/n7=2-136.
DR PDB; 5DGE; X-ray; 3.45 A; N7/n7=2-136.
DR PDB; 5DGF; X-ray; 3.30 A; N7/n7=2-136.
DR PDB; 5DGV; X-ray; 3.10 A; N7/n7=2-136.
DR PDB; 5FCI; X-ray; 3.40 A; N7/n7=2-136.
DR PDB; 5FCJ; X-ray; 3.10 A; N7/n7=2-136.
DR PDB; 5FL8; EM; 9.50 A; Z=1-136.
DR PDB; 5GAK; EM; 3.88 A; b=1-136.
DR PDB; 5H4P; EM; 3.07 A; Z=1-136.
DR PDB; 5I4L; X-ray; 3.10 A; N7/n7=2-136.
DR PDB; 5JCS; EM; 9.50 A; Z=1-136.
DR PDB; 5JUO; EM; 4.00 A; EA=1-136.
DR PDB; 5JUP; EM; 3.50 A; EA=1-136.
DR PDB; 5JUS; EM; 4.20 A; EA=1-136.
DR PDB; 5JUT; EM; 4.00 A; EA=1-136.
DR PDB; 5JUU; EM; 4.00 A; EA=1-136.
DR PDB; 5LYB; X-ray; 3.25 A; N7/n7=2-136.
DR PDB; 5M1J; EM; 3.30 A; Z5=2-136.
DR PDB; 5MC6; EM; 3.80 A; AN=1-136.
DR PDB; 5MEI; X-ray; 3.50 A; AA/DB=2-136.
DR PDB; 5NDG; X-ray; 3.70 A; N7/n7=2-136.
DR PDB; 5NDV; X-ray; 3.30 A; N7/n7=2-136.
DR PDB; 5NDW; X-ray; 3.70 A; N7/n7=2-136.
DR PDB; 5OBM; X-ray; 3.40 A; N7/n7=2-136.
DR PDB; 5ON6; X-ray; 3.10 A; AA/DB=2-136.
DR PDB; 5T62; EM; 3.30 A; m=1-136.
DR PDB; 5T6R; EM; 4.50 A; m=1-136.
DR PDB; 5TBW; X-ray; 3.00 A; AA/DB=2-136.
DR PDB; 5TGA; X-ray; 3.30 A; N7/n7=2-136.
DR PDB; 5TGM; X-ray; 3.50 A; N7/n7=2-136.
DR PDB; 6CB1; EM; 4.60 A; Z=1-136.
DR PDB; 6ELZ; EM; 3.30 A; Z=1-136.
DR PDB; 6EM5; EM; 4.30 A; Z=1-136.
DR PDB; 6FT6; EM; 3.90 A; Z=1-136.
DR PDB; 6GQ1; EM; 4.40 A; Z=2-136.
DR PDB; 6GQB; EM; 3.90 A; Z=2-136.
DR PDB; 6GQV; EM; 4.00 A; Z=2-136.
DR PDB; 6HD7; EM; 3.40 A; b=1-136.
DR PDB; 6HHQ; X-ray; 3.10 A; AA/DB=1-136.
DR PDB; 6I7O; EM; 5.30 A; AN/XN=2-136.
DR PDB; 6M62; EM; 3.20 A; Z=1-136.
DR PDB; 6N8J; EM; 3.50 A; Z=1-136.
DR PDB; 6N8K; EM; 3.60 A; Z=1-136.
DR PDB; 6N8L; EM; 3.60 A; Z=1-136.
DR PDB; 6N8M; EM; 3.50 A; m=1-136.
DR PDB; 6N8N; EM; 3.80 A; m=1-136.
DR PDB; 6N8O; EM; 3.50 A; m=1-136.
DR PDB; 6OIG; EM; 3.80 A; Z=2-136.
DR PDB; 6Q8Y; EM; 3.10 A; AN=2-136.
DR PDB; 6QIK; EM; 3.10 A; Y=1-136.
DR PDB; 6QT0; EM; 3.40 A; Y=1-136.
DR PDB; 6QTZ; EM; 3.50 A; Y=1-136.
DR PDB; 6R84; EM; 3.60 A; b=2-136.
DR PDB; 6R86; EM; 3.40 A; b=2-136.
DR PDB; 6R87; EM; 3.40 A; b=2-136.
DR PDB; 6RI5; EM; 3.30 A; Y=1-136.
DR PDB; 6RZZ; EM; 3.20 A; Y=1-136.
DR PDB; 6S05; EM; 3.90 A; Y=1-136.
DR PDB; 6S47; EM; 3.28 A; Ab=2-136.
DR PDB; 6SNT; EM; 2.80 A; aq=1-136.
DR PDB; 6SV4; EM; 3.30 A; AN/XN/zN=1-136.
DR PDB; 6T4Q; EM; 2.60 A; LZ=2-136.
DR PDB; 6T7I; EM; 3.20 A; LZ=1-136.
DR PDB; 6T7T; EM; 3.10 A; LZ=1-136.
DR PDB; 6T83; EM; 4.00 A; K/Zy=1-136.
DR PDB; 6TB3; EM; 2.80 A; AN=2-136.
DR PDB; 6TNU; EM; 3.10 A; AN=2-136.
DR PDB; 6WOO; EM; 2.90 A; Z=3-136.
DR PDB; 6XIQ; EM; 4.20 A; Z=1-136.
DR PDB; 6XIR; EM; 3.20 A; Z=1-136.
DR PDB; 6YLG; EM; 3.00 A; Z=1-136.
DR PDB; 6YLH; EM; 3.10 A; Z=1-136.
DR PDB; 6YLX; EM; 3.90 A; Z=1-136.
DR PDB; 6YLY; EM; 3.80 A; Z=1-136.
DR PDB; 6Z6J; EM; 3.40 A; LZ=1-136.
DR PDB; 6Z6K; EM; 3.40 A; LZ=1-136.
DR PDB; 7AZY; EM; 2.88 A; O=1-136.
DR PDB; 7B7D; EM; 3.30 A; LV=2-136.
DR PDB; 7BT6; EM; 3.12 A; Z=1-136.
DR PDB; 7BTB; EM; 3.22 A; Z=1-136.
DR PDB; 7NRC; EM; 3.90 A; Lb=2-136.
DR PDB; 7NRD; EM; 4.36 A; Lb=2-136.
DR PDB; 7OF1; EM; 3.10 A; Z=1-136.
DR PDB; 7OH3; EM; 3.40 A; Z=1-136.
DR PDB; 7OHQ; EM; 3.10 A; Z=1-136.
DR PDB; 7OHR; EM; 4.72 A; Z=1-136.
DR PDB; 7OHV; EM; 3.90 A; Z=1-136.
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; 4V6I; -.
DR PDBsum; 4V7F; -.
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; 6CB1; -.
DR PDBsum; 6ELZ; -.
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; 6WOO; -.
DR PDBsum; 6XIQ; -.
DR PDBsum; 6XIR; -.
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; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHV; -.
DR AlphaFoldDB; P0C2H6; -.
DR SMR; P0C2H6; -.
DR BioGRID; 36437; 133.
DR IntAct; P0C2H6; 8.
DR MINT; P0C2H6; -.
DR STRING; 4932.YHR010W; -.
DR iPTMnet; P0C2H6; -.
DR MaxQB; P0C2H6; -.
DR PaxDb; P0C2H6; -.
DR PRIDE; P0C2H6; -.
DR TopDownProteomics; P0C2H6; -.
DR EnsemblFungi; YHR010W_mRNA; YHR010W; YHR010W.
DR GeneID; 856401; -.
DR KEGG; sce:YHR010W; -.
DR SGD; S000001052; RPL27A.
DR VEuPathDB; FungiDB:YHR010W; -.
DR eggNOG; KOG3418; Eukaryota.
DR GeneTree; ENSGT00390000010721; -.
DR HOGENOM; CLU_067359_0_1_1; -.
DR InParanoid; P0C2H6; -.
DR OMA; HPFPYAI; -.
DR BioCyc; YEAST:G3O-31073-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-72689; Formation of a pool of free 40S subunits.
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:P0C2H6; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P0C2H6; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR CDD; cd06090; KOW_RPL27; 1.
DR Gene3D; 2.30.30.770; -; 1.
DR InterPro; IPR041991; KOW_RPL27.
DR InterPro; IPR038655; L27e_sf.
DR InterPro; IPR001141; Ribosomal_L27e.
DR InterPro; IPR018262; Ribosomal_L27e_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR10497; PTHR10497; 1.
DR Pfam; PF01777; Ribosomal_L27e; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR PROSITE; PS01107; RIBOSOMAL_L27E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260"
FT CHAIN 2..136
FT /note="60S ribosomal protein L27-A"
FT /id="PRO_0000126092"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:4U56"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4U4N"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 104..122
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 123..127
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 136 AA; 15531 MW; F3924B039AA2D85D CRC64;
MAKFLKAGKV AVVVRGRYAG KKVVIVKPHD EGSKSHPFGH ALVAGIERYP LKVTKKHGAK
KVAKRTKIKP FIKVVNYNHL LPTRYTLDVE AFKSVVSTET FEQPSQREEA KKVVKKAFEE
RHQAGKNQWF FSKLRF
