RL31A_YEAST
ID RL31A_YEAST Reviewed; 113 AA.
AC P0C2H8; D6VRS4; P04649; Q3E7B8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=60S ribosomal protein L31-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L34;
DE AltName: Full=Large ribosomal subunit protein eL31-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YL28;
GN Name=RPL31A {ECO:0000303|PubMed:9559554}; Synonyms=RPL34, RPL34A;
GN OrderedLocusNames=YDL075W; ORFNames=D2478;
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=Carlsbergensis;
RA Schaap P.J., Molenaar C.M.T., Mager W.H., Planta R.J.;
RT "The primary structure of a gene encoding yeast ribosomal protein L34.";
RL Curr. Genet. 9:47-52(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 PARTIAL PROTEIN SEQUENCE OF 2-51, AND CLEAVAGE OF INITIATOR METHIONINE.
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 [5]
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 [6]
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 [7]
RP 3D-STRUCTURE MODELING OF 6-83, 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 [8]
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 [9]
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 [10]
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 [11]
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:22096102}.
CC -!- MISCELLANEOUS: There are 2 genes for eL31 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL31 family.
CC {ECO:0000305}.
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DR EMBL; X01441; CAA25679.1; -; Genomic_DNA.
DR EMBL; Z74123; CAA98641.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11784.1; -; Genomic_DNA.
DR PIR; S67611; R5BY1E.
DR RefSeq; NP_010208.1; NM_001180134.1.
DR PDB; 2WW9; EM; 8.60 A; M=1-113.
DR PDB; 2WWA; EM; 8.90 A; M=1-113.
DR PDB; 2WWB; EM; 6.48 A; M=1-113.
DR PDB; 3J6X; EM; 6.10 A; 71=1-113.
DR PDB; 3J6Y; EM; 6.10 A; 71=1-113.
DR PDB; 3J77; EM; 6.20 A; 81=1-113.
DR PDB; 3J78; EM; 6.30 A; 81=1-113.
DR PDB; 3JCT; EM; 3.08 A; d=1-113.
DR PDB; 4U3M; X-ray; 3.00 A; O1/o1=2-113.
DR PDB; 4U3N; X-ray; 3.20 A; O1/o1=2-113.
DR PDB; 4U3U; X-ray; 2.90 A; O1/o1=2-113.
DR PDB; 4U4N; X-ray; 3.10 A; O1/o1=2-113.
DR PDB; 4U4O; X-ray; 3.60 A; O1/o1=2-113.
DR PDB; 4U4Q; X-ray; 3.00 A; O1/o1=2-113.
DR PDB; 4U4R; X-ray; 2.80 A; O1/o1=2-113.
DR PDB; 4U4U; X-ray; 3.00 A; O1/o1=2-113.
DR PDB; 4U4Y; X-ray; 3.20 A; O1/o1=2-113.
DR PDB; 4U4Z; X-ray; 3.10 A; O1/o1=2-113.
DR PDB; 4U50; X-ray; 3.20 A; O1/o1=2-113.
DR PDB; 4U51; X-ray; 3.20 A; O1/o1=2-113.
DR PDB; 4U52; X-ray; 3.00 A; O1/o1=2-113.
DR PDB; 4U53; X-ray; 3.30 A; O1/o1=2-113.
DR PDB; 4U55; X-ray; 3.20 A; O1/o1=2-113.
DR PDB; 4U56; X-ray; 3.45 A; O1/o1=2-113.
DR PDB; 4U6F; X-ray; 3.10 A; O1/o1=2-113.
DR PDB; 4V4B; EM; 11.70 A; BW=2-113.
DR PDB; 4V6I; EM; 8.80 A; Bg=1-113.
DR PDB; 4V7F; EM; 8.70 A; c=1-113.
DR PDB; 4V7R; X-ray; 4.00 A; Ba/Da=1-113.
DR PDB; 4V88; X-ray; 3.00 A; Bd/Dd=1-113.
DR PDB; 4V8T; EM; 8.10 A; d=1-113.
DR PDB; 4V8Y; EM; 4.30 A; Bd=2-113.
DR PDB; 4V8Z; EM; 6.60 A; Bd=2-113.
DR PDB; 4V91; EM; 3.70 A; d=1-113.
DR PDB; 5APN; EM; 3.91 A; d=1-113.
DR PDB; 5APO; EM; 3.41 A; d=1-113.
DR PDB; 5DAT; X-ray; 3.15 A; O1/o1=2-113.
DR PDB; 5DC3; X-ray; 3.25 A; O1/o1=2-113.
DR PDB; 5DGE; X-ray; 3.45 A; O1/o1=2-113.
DR PDB; 5DGF; X-ray; 3.30 A; O1/o1=2-113.
DR PDB; 5DGV; X-ray; 3.10 A; O1/o1=2-113.
DR PDB; 5FCI; X-ray; 3.40 A; O1/o1=2-113.
DR PDB; 5FCJ; X-ray; 3.10 A; O1/o1=2-113.
DR PDB; 5FL8; EM; 9.50 A; d=1-113.
DR PDB; 5GAK; EM; 3.88 A; f=4-112.
DR PDB; 5H4P; EM; 3.07 A; d=1-113.
DR PDB; 5I4L; X-ray; 3.10 A; O1/o1=4-112.
DR PDB; 5JCS; EM; 9.50 A; d=1-113.
DR PDB; 5JUO; EM; 4.00 A; IA=1-113.
DR PDB; 5JUP; EM; 3.50 A; IA=1-113.
DR PDB; 5JUS; EM; 4.20 A; IA=1-113.
DR PDB; 5JUT; EM; 4.00 A; IA=1-113.
DR PDB; 5JUU; EM; 4.00 A; IA=1-113.
DR PDB; 5LYB; X-ray; 3.25 A; O1/o1=4-112.
DR PDB; 5M1J; EM; 3.30 A; d5=4-112.
DR PDB; 5MC6; EM; 3.80 A; BC=1-113.
DR PDB; 5MEI; X-ray; 3.50 A; AE/DF=4-112.
DR PDB; 5NDG; X-ray; 3.70 A; O1/o1=4-112.
DR PDB; 5NDV; X-ray; 3.30 A; O1/o1=2-113.
DR PDB; 5NDW; X-ray; 3.70 A; O1/o1=4-112.
DR PDB; 5OBM; X-ray; 3.40 A; O1/o1=4-112.
DR PDB; 5ON6; X-ray; 3.10 A; AE/DF=4-112.
DR PDB; 5T62; EM; 3.30 A; q=1-113.
DR PDB; 5T6R; EM; 4.50 A; q=1-113.
DR PDB; 5TBW; X-ray; 3.00 A; AE/DF=4-112.
DR PDB; 5TGA; X-ray; 3.30 A; O1/o1=4-112.
DR PDB; 5TGM; X-ray; 3.50 A; O1/o1=4-112.
DR PDB; 6ELZ; EM; 3.30 A; d=1-113.
DR PDB; 6EM5; EM; 4.30 A; d=1-113.
DR PDB; 6FT6; EM; 3.90 A; d=1-113.
DR PDB; 6GQ1; EM; 4.40 A; d=4-112.
DR PDB; 6GQB; EM; 3.90 A; d=4-112.
DR PDB; 6GQV; EM; 4.00 A; d=4-112.
DR PDB; 6HD7; EM; 3.40 A; f=4-112.
DR PDB; 6HHQ; X-ray; 3.10 A; AE/DF=1-113.
DR PDB; 6I7O; EM; 5.30 A; BC/YC=4-112.
DR PDB; 6M62; EM; 3.20 A; d=1-113.
DR PDB; 6N8J; EM; 3.50 A; d=1-113.
DR PDB; 6N8K; EM; 3.60 A; d=1-113.
DR PDB; 6N8L; EM; 3.60 A; d=1-113.
DR PDB; 6N8M; EM; 3.50 A; q=1-113.
DR PDB; 6N8N; EM; 3.80 A; q=1-113.
DR PDB; 6N8O; EM; 3.50 A; q=1-113.
DR PDB; 6OIG; EM; 3.80 A; d=4-112.
DR PDB; 6Q8Y; EM; 3.10 A; BC=4-112.
DR PDB; 6QIK; EM; 3.10 A; d=1-113.
DR PDB; 6QT0; EM; 3.40 A; d=1-113.
DR PDB; 6QTZ; EM; 3.50 A; d=1-113.
DR PDB; 6R84; EM; 3.60 A; f=4-112.
DR PDB; 6R86; EM; 3.40 A; f=4-112.
DR PDB; 6R87; EM; 3.40 A; f=4-112.
DR PDB; 6RI5; EM; 3.30 A; d=1-113.
DR PDB; 6RZZ; EM; 3.20 A; d=1-113.
DR PDB; 6S05; EM; 3.90 A; d=1-113.
DR PDB; 6S47; EM; 3.28 A; Af=2-113.
DR PDB; 6SNT; EM; 2.80 A; am=1-113.
DR PDB; 6SV4; EM; 3.30 A; BC/YC/ZC=1-113.
DR PDB; 6T4Q; EM; 2.60 A; Ld=4-112.
DR PDB; 6T7I; EM; 3.20 A; Ld=1-113.
DR PDB; 6T7T; EM; 3.10 A; Ld=1-113.
DR PDB; 6T83; EM; 4.00 A; O/dy=1-113.
DR PDB; 6TB3; EM; 2.80 A; BC=4-112.
DR PDB; 6TNU; EM; 3.10 A; BC=4-112.
DR PDB; 6WOO; EM; 2.90 A; d=5-110.
DR PDB; 6XIQ; EM; 4.20 A; d=1-113.
DR PDB; 6XIR; EM; 3.20 A; d=1-113.
DR PDB; 6YLG; EM; 3.00 A; d=1-113.
DR PDB; 6YLH; EM; 3.10 A; d=1-113.
DR PDB; 6YLX; EM; 3.90 A; d=1-113.
DR PDB; 6YLY; EM; 3.80 A; d=1-113.
DR PDB; 6Z6J; EM; 3.40 A; Ld=1-113.
DR PDB; 6Z6K; EM; 3.40 A; Ld=1-113.
DR PDB; 7AZY; EM; 2.88 A; n=1-113.
DR PDB; 7B7D; EM; 3.30 A; LZ=4-112.
DR PDB; 7BT6; EM; 3.12 A; d=1-113.
DR PDB; 7BTB; EM; 3.22 A; d=1-113.
DR PDB; 7NRC; EM; 3.90 A; Lf=4-112.
DR PDB; 7NRD; EM; 4.36 A; Lf=4-112.
DR PDB; 7OF1; EM; 3.10 A; d=1-113.
DR PDB; 7OH3; EM; 3.40 A; d=1-113.
DR PDB; 7OHQ; EM; 3.10 A; d=1-113.
DR PDB; 7OHR; EM; 4.72 A; d=1-113.
DR PDB; 7OHV; EM; 3.90 A; d=1-113.
DR PDBsum; 2WW9; -.
DR PDBsum; 2WWA; -.
DR PDBsum; 2WWB; -.
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; 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; P0C2H8; -.
DR SMR; P0C2H8; -.
DR BioGRID; 31986; 583.
DR DIP; DIP-5135N; -.
DR IntAct; P0C2H8; 5.
DR MINT; P0C2H8; -.
DR STRING; 4932.YDL075W; -.
DR CarbonylDB; P0C2H8; -.
DR iPTMnet; P0C2H8; -.
DR MaxQB; P0C2H8; -.
DR PaxDb; P0C2H8; -.
DR PRIDE; P0C2H8; -.
DR TopDownProteomics; P0C2H8; -.
DR EnsemblFungi; YDL075W_mRNA; YDL075W; YDL075W.
DR GeneID; 851484; -.
DR KEGG; sce:YDL075W; -.
DR SGD; S000002233; RPL31A.
DR VEuPathDB; FungiDB:YDL075W; -.
DR eggNOG; KOG0893; Eukaryota.
DR GeneTree; ENSGT00950000183030; -.
DR HOGENOM; CLU_112570_1_1_1; -.
DR InParanoid; P0C2H8; -.
DR OMA; KTMKTHN; -.
DR BioCyc; YEAST:G3O-29486-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 EvolutionaryTrace; P0C2H8; -.
DR PRO; PR:P0C2H8; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P0C2H8; 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; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:SGD.
DR GO; GO:0006450; P:regulation of translational fidelity; IMP:SGD.
DR CDD; cd00463; Ribosomal_L31e; 1.
DR Gene3D; 3.10.440.10; -; 1.
DR InterPro; IPR000054; Ribosomal_L31e.
DR InterPro; IPR020052; Ribosomal_L31e_CS.
DR InterPro; IPR023621; Ribosomal_L31e_dom_sf.
DR PANTHER; PTHR10956; PTHR10956; 1.
DR Pfam; PF01198; Ribosomal_L31e; 1.
DR SMART; SM01380; Ribosomal_L31e; 1.
DR SUPFAM; SSF54575; SSF54575; 1.
DR PROSITE; PS01144; RIBOSOMAL_L31E; 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:18782943"
FT CHAIN 2..113
FT /note="60S ribosomal protein L31-A"
FT /id="PRO_0000153788"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 28..44
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4U6F"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4U4Q"
SQ SEQUENCE 113 AA; 12953 MW; 351B5ADD15DB3B5D CRC64;
MAGLKDVVTR EYTINLHKRL HGVSFKKRAP RAVKEIKKFA KLHMGTDDVR LAPELNQAIW
KRGVKGVEYR LRLRISRKRN EEEDAKNPLF SYVEPVLVAS AKGLQTVVVE EDA
