RL8A_YEAST
ID RL8A_YEAST Reviewed; 256 AA.
AC P17076; D3DKT5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=60S ribosomal protein L8-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L4;
DE AltName: Full=L4-2;
DE AltName: Full=L7a-1;
DE AltName: Full=Large ribosomal subunit protein eL8-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=Maintenance of killer protein 7;
DE AltName: Full=RP6;
DE AltName: Full=YL5;
GN Name=RPL8A {ECO:0000303|PubMed:9559554}; Synonyms=MAK7, RPL4A;
GN OrderedLocusNames=YHL033C;
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 204508 / S288c;
RX PubMed=2046660; DOI=10.1007/bf00260709;
RA Yon J., Giallongo A., Fried M.;
RT "The organization and expression of the Saccharomyces cerevisiae L4
RT ribosomal protein genes and their identification as the homologues of the
RT mammalian ribosomal protein gene L7a.";
RL Mol. Gen. Genet. 227:72-80(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204626 / S288c / A364A;
RX PubMed=2183194; DOI=10.1093/nar/18.6.1447;
RA Arevalo S.G., Warner J.R.;
RT "Ribosomal protein L4 of Saccharomyces cerevisiae: the gene and its
RT protein.";
RL Nucleic Acids Res. 18:1447-1450(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=787537; DOI=10.1016/0022-2836(76)90102-9;
RA Wickner R.B., Leibowitz M.J.;
RT "Chromosomal genes essential for replication of a double-stranded RNA
RT plasmid of Saccharomyces cerevisiae: the killer character of yeast.";
RL J. Mol. Biol. 105:427-443(1976).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-20.
RX PubMed=1544921; DOI=10.1016/s0021-9258(18)42785-8;
RA Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
RT "NH2-terminal acetylation of ribosomal proteins of Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 267:5442-5445(1992).
RN [7]
RP IDENTIFICATION AS MAK7.
RX PubMed=7739558; DOI=10.1128/mcb.15.5.2772;
RA Ohtake Y., Wickner R.B.;
RT "Yeast virus propagation depends critically on free 60S ribosomal subunit
RT concentration.";
RL Mol. Cell. Biol. 15:2772-2781(1995).
RN [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
RP 3D-STRUCTURE MODELING OF 102-220, 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 [14]
RP 3D-STRUCTURE MODELING OF 102-220, 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 [15]
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 [16]
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 238000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eL8 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 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; X17204; CAA35073.1; -; Genomic_DNA.
DR EMBL; X56836; CAA40166.1; -; Genomic_DNA.
DR EMBL; U17361; AAA64574.1; -; Genomic_DNA.
DR EMBL; U11583; AAB65045.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06652.1; -; Genomic_DNA.
DR PIR; S16811; R5BY7A.
DR RefSeq; NP_011830.1; NM_001179113.1.
DR PDB; 3J6X; EM; 6.10 A; L8=1-256.
DR PDB; 3J6Y; EM; 6.10 A; L8=1-256.
DR PDB; 3J77; EM; 6.20 A; L8=1-256.
DR PDB; 3J78; EM; 6.30 A; L8=1-256.
DR PDB; 3JCT; EM; 3.08 A; G=1-256.
DR PDB; 4U3M; X-ray; 3.00 A; L8/l8=2-256.
DR PDB; 4U3N; X-ray; 3.20 A; L8/l8=2-256.
DR PDB; 4U3U; X-ray; 2.90 A; L8/l8=2-256.
DR PDB; 4U4N; X-ray; 3.10 A; L8/l8=2-256.
DR PDB; 4U4O; X-ray; 3.60 A; L8/l8=2-256.
DR PDB; 4U4Q; X-ray; 3.00 A; L8/l8=2-256.
DR PDB; 4U4R; X-ray; 2.80 A; L8/l8=2-256.
DR PDB; 4U4U; X-ray; 3.00 A; L8/l8=2-256.
DR PDB; 4U4Y; X-ray; 3.20 A; L8/l8=2-256.
DR PDB; 4U4Z; X-ray; 3.10 A; L8/l8=2-256.
DR PDB; 4U50; X-ray; 3.20 A; L8/l8=2-256.
DR PDB; 4U51; X-ray; 3.20 A; L8/l8=2-256.
DR PDB; 4U52; X-ray; 3.00 A; L8/l8=2-256.
DR PDB; 4U53; X-ray; 3.30 A; L8/l8=2-256.
DR PDB; 4U55; X-ray; 3.20 A; L8/l8=2-256.
DR PDB; 4U56; X-ray; 3.45 A; L8/l8=2-256.
DR PDB; 4U6F; X-ray; 3.10 A; L8/l8=2-256.
DR PDB; 4V4B; EM; 11.70 A; BG=102-220.
DR PDB; 4V6I; EM; 8.80 A; BH=1-256.
DR PDB; 4V7F; EM; 8.70 A; H=1-256.
DR PDB; 4V7R; X-ray; 4.00 A; BH/DH=1-256.
DR PDB; 4V88; X-ray; 3.00 A; BG/DG=1-256.
DR PDB; 4V8T; EM; 8.10 A; G=1-256.
DR PDB; 4V8Y; EM; 4.30 A; BG=2-256.
DR PDB; 4V8Z; EM; 6.60 A; BG=2-256.
DR PDB; 4V91; EM; 3.70 A; G=1-256.
DR PDB; 5APN; EM; 3.91 A; G=1-256.
DR PDB; 5APO; EM; 3.41 A; G=1-256.
DR PDB; 5DAT; X-ray; 3.15 A; L8/l8=2-256.
DR PDB; 5DC3; X-ray; 3.25 A; L8/l8=2-256.
DR PDB; 5DGE; X-ray; 3.45 A; L8/l8=2-256.
DR PDB; 5DGF; X-ray; 3.30 A; L8/l8=2-256.
DR PDB; 5FCI; X-ray; 3.40 A; L8/l8=2-256.
DR PDB; 5FCJ; X-ray; 3.10 A; L8/l8=2-256.
DR PDB; 5FL8; EM; 9.50 A; G=1-256.
DR PDB; 5GAK; EM; 3.88 A; K=1-256.
DR PDB; 5H4P; EM; 3.07 A; G=1-256.
DR PDB; 5I4L; X-ray; 3.10 A; L8=24-256, l8=24-254.
DR PDB; 5JCS; EM; 9.50 A; G=1-256.
DR PDB; 5JUO; EM; 4.00 A; L=1-256.
DR PDB; 5JUP; EM; 3.50 A; L=1-256.
DR PDB; 5JUS; EM; 4.20 A; L=1-256.
DR PDB; 5JUT; EM; 4.00 A; L=1-256.
DR PDB; 5JUU; EM; 4.00 A; L=1-256.
DR PDB; 5LYB; X-ray; 3.25 A; L8=24-256, l8=24-248.
DR PDB; 5M1J; EM; 3.30 A; G5=24-256.
DR PDB; 5MC6; EM; 3.80 A; AA=1-256.
DR PDB; 5MEI; X-ray; 3.50 A; CJ/p=24-256.
DR PDB; 5NDG; X-ray; 3.70 A; L8/l8=24-256.
DR PDB; 5NDV; X-ray; 3.30 A; L8/l8=24-254.
DR PDB; 5NDW; X-ray; 3.70 A; L8/l8=24-256.
DR PDB; 5OBM; X-ray; 3.40 A; L8/l8=24-256.
DR PDB; 5ON6; X-ray; 3.10 A; CJ/p=24-256.
DR PDB; 5T62; EM; 3.30 A; J=1-256.
DR PDB; 5T6R; EM; 4.50 A; J=1-256.
DR PDB; 5TBW; X-ray; 3.00 A; CJ/p=24-256.
DR PDB; 5TGA; X-ray; 3.30 A; L8/l8=24-256.
DR PDB; 5TGM; X-ray; 3.50 A; L8=24-256, l8=24-248.
DR PDB; 5Z3G; EM; 3.65 A; K=1-256.
DR PDB; 6C0F; EM; 3.70 A; G=1-256.
DR PDB; 6CB1; EM; 4.60 A; G=1-256.
DR PDB; 6ELZ; EM; 3.30 A; G=1-256.
DR PDB; 6EM1; EM; 3.60 A; G=1-256.
DR PDB; 6EM3; EM; 3.20 A; G=1-256.
DR PDB; 6EM4; EM; 4.10 A; G=1-256.
DR PDB; 6EM5; EM; 4.30 A; G=1-256.
DR PDB; 6FT6; EM; 3.90 A; G=1-256.
DR PDB; 6GQ1; EM; 4.40 A; G=24-256.
DR PDB; 6GQB; EM; 3.90 A; G=24-256.
DR PDB; 6GQV; EM; 4.00 A; G=24-256.
DR PDB; 6HD7; EM; 3.40 A; K=1-256.
DR PDB; 6HHQ; X-ray; 3.10 A; CJ/p=1-256.
DR PDB; 6I7O; EM; 5.30 A; AA/XA=24-254.
DR PDB; 6M62; EM; 3.20 A; G=1-256.
DR PDB; 6N8J; EM; 3.50 A; G=1-256.
DR PDB; 6N8K; EM; 3.60 A; G=1-256.
DR PDB; 6N8L; EM; 3.60 A; G=1-256.
DR PDB; 6N8M; EM; 3.50 A; J=1-256.
DR PDB; 6N8N; EM; 3.80 A; J=1-256.
DR PDB; 6N8O; EM; 3.50 A; J=1-256.
DR PDB; 6OIG; EM; 3.80 A; G=24-256.
DR PDB; 6Q8Y; EM; 3.10 A; AA=24-256.
DR PDB; 6QIK; EM; 3.10 A; H=1-256.
DR PDB; 6QT0; EM; 3.40 A; H=1-256.
DR PDB; 6QTZ; EM; 3.50 A; H=1-256.
DR PDB; 6R84; EM; 3.60 A; K=24-256.
DR PDB; 6R86; EM; 3.40 A; K=24-256.
DR PDB; 6R87; EM; 3.40 A; K=24-256.
DR PDB; 6RI5; EM; 3.30 A; H=1-256.
DR PDB; 6RZZ; EM; 3.20 A; H=1-256.
DR PDB; 6S05; EM; 3.90 A; H=1-256.
DR PDB; 6S47; EM; 3.28 A; AJ=24-256.
DR PDB; 6SNT; EM; 2.80 A; n=1-256.
DR PDB; 6SV4; EM; 3.30 A; AA/XA/zA=1-256.
DR PDB; 6T4Q; EM; 2.60 A; LG=24-256.
DR PDB; 6T7I; EM; 3.20 A; LG=1-256.
DR PDB; 6T7T; EM; 3.10 A; LG=1-256.
DR PDB; 6T83; EM; 4.00 A; Gy/Ja=1-256.
DR PDB; 6TB3; EM; 2.80 A; AA=24-256.
DR PDB; 6TNU; EM; 3.10 A; AA=24-256.
DR PDB; 6WOO; EM; 2.90 A; G=24-256.
DR PDB; 6YLG; EM; 3.00 A; G=1-256.
DR PDB; 6YLH; EM; 3.10 A; G=1-256.
DR PDB; 6YLX; EM; 3.90 A; G=1-256.
DR PDB; 6YLY; EM; 3.80 A; G=1-256.
DR PDB; 6Z6J; EM; 3.40 A; LG=1-256.
DR PDB; 6Z6K; EM; 3.40 A; LG=1-256.
DR PDB; 7AZY; EM; 2.88 A; b=1-256.
DR PDB; 7B7D; EM; 3.30 A; LJ=24-256.
DR PDB; 7BT6; EM; 3.12 A; G=1-256.
DR PDB; 7BTB; EM; 3.22 A; G=1-256.
DR PDB; 7NRC; EM; 3.90 A; LJ=24-256.
DR PDB; 7NRD; EM; 4.36 A; LJ=24-256.
DR PDB; 7OF1; EM; 3.10 A; G=1-256.
DR PDB; 7OH3; EM; 3.40 A; G=1-256.
DR PDB; 7OHP; EM; 3.90 A; G=1-256.
DR PDB; 7OHQ; EM; 3.10 A; G=1-256.
DR PDB; 7OHR; EM; 4.72 A; G=1-256.
DR PDB; 7OHS; EM; 4.38 A; G=1-256.
DR PDB; 7OHU; EM; 3.70 A; G=1-256.
DR PDB; 7OHV; EM; 3.90 A; G=1-256.
DR PDB; 7OHW; EM; 3.50 A; G=1-256.
DR PDB; 7OHX; EM; 3.30 A; G=1-256.
DR PDB; 7OHY; EM; 3.90 A; G=1-256.
DR PDB; 7OSA; X-ray; 3.00 A; eL8=1-256.
DR PDB; 7OSM; X-ray; 3.00 A; eL8=1-256.
DR PDB; 7RR5; EM; 3.23 A; LG=1-256.
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; 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; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
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; 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; 7OHU; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR PDBsum; 7OHY; -.
DR PDBsum; 7OSA; -.
DR PDBsum; 7OSM; -.
DR PDBsum; 7RR5; -.
DR AlphaFoldDB; P17076; -.
DR SMR; P17076; -.
DR BioGRID; 36389; 420.
DR DIP; DIP-5102N; -.
DR IntAct; P17076; 43.
DR MINT; P17076; -.
DR STRING; 4932.YHL033C; -.
DR CarbonylDB; P17076; -.
DR iPTMnet; P17076; -.
DR MaxQB; P17076; -.
DR PaxDb; P17076; -.
DR PRIDE; P17076; -.
DR EnsemblFungi; YHL033C_mRNA; YHL033C; YHL033C.
DR GeneID; 856352; -.
DR KEGG; sce:YHL033C; -.
DR SGD; S000001025; RPL8A.
DR VEuPathDB; FungiDB:YHL033C; -.
DR eggNOG; KOG3166; Eukaryota.
DR GeneTree; ENSGT00940000170054; -.
DR HOGENOM; CLU_055193_0_0_1; -.
DR InParanoid; P17076; -.
DR OMA; DDFKEVQ; -.
DR BioCyc; YEAST:G3O-31052-MON; -.
DR EvolutionaryTrace; P17076; -.
DR PRO; PR:P17076; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P17076; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IC:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IMP:SGD.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR001921; Ribosomal_L7A/L8.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR InterPro; IPR004037; Ribosomal_L7Ae_CS.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00882; RIBOSOMALL7A.
DR SUPFAM; SSF55315; SSF55315; 1.
DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921"
FT CHAIN 2..256
FT /note="60S ribosomal protein L8-A"
FT /id="PRO_0000136760"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 113
FT /note="A -> R (in Ref. 2; CAA35073)"
FT /evidence="ECO:0000305"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 222..226
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 256 AA; 28125 MW; E3C8537D8683C905 CRC64;
MAPGKKVAPA PFGAKSTKSN KTRNPLTHST PKNFGIGQAV QPKRNLSRYV KWPEYVRVQR
QKKILSIRLK VPPTIAQFQY TLDRNTAAET FKLFNKYRPE TAAEKKERLT KEAAAVAEGK
SKQDASPKPY AVKYGLNHVV ALIENKKAKL VLIANDVDPI ELVVFLPALC KKMGVPYAIV
KGKARLGTLV NQKTSAVAAL TEVRAEDEAA LAKLVSTIDA NFADKYDEVK KHWGGGILGN
KAQAKMDKRA KNSDSA
