RL33A_YEAST
ID RL33A_YEAST Reviewed; 107 AA.
AC P05744; D6W3M6;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=60S ribosomal protein L33-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L37;
DE AltName: Full=Large ribosomal subunit protein eL33-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=RP47;
DE AltName: Full=YL37;
GN Name=RPL33A {ECO:0000303|PubMed:9559554}; Synonyms=RPL37A;
GN OrderedLocusNames=YPL143W; ORFNames=LPI4W, P2625;
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 204626 / S288c / A364A;
RX PubMed=1840541; DOI=10.1016/0378-1119(91)90526-h;
RA Santangelo G.M., Tornow J., McLaughlin C.S., Moldave K.;
RT "Screening a yeast promoter library leads to the isolation of the RP29/L32
RT and SNR17B/RPL37A divergent promoters and the discovery of a gene encoding
RT ribosomal protein L37.";
RL Gene 105:137-138(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 2-26, 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 [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 CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT ALA-2 BY NATA.
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 [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-47, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
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 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 -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260}.
CC -!- MISCELLANEOUS: There are 2 genes for eL33 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL33 family.
CC {ECO:0000305}.
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DR EMBL; X57969; CAA41035.1; -; Genomic_DNA.
DR EMBL; U43703; AAB68218.1; -; Genomic_DNA.
DR EMBL; Z73499; CAA97847.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11292.1; -; Genomic_DNA.
DR PIR; S18431; S18431.
DR RefSeq; NP_015182.1; NM_001183957.1.
DR PDB; 3J6X; EM; 6.10 A; 73=1-107.
DR PDB; 3J6Y; EM; 6.10 A; 73=1-107.
DR PDB; 3J77; EM; 6.20 A; 83=1-107.
DR PDB; 3J78; EM; 6.30 A; 83=1-107.
DR PDB; 3JCT; EM; 3.08 A; f=1-107.
DR PDB; 4U3M; X-ray; 3.00 A; O3/o3=2-107.
DR PDB; 4U3N; X-ray; 3.20 A; O3/o3=2-107.
DR PDB; 4U3U; X-ray; 2.90 A; O3/o3=2-107.
DR PDB; 4U4N; X-ray; 3.10 A; O3/o3=2-107.
DR PDB; 4U4O; X-ray; 3.60 A; O3/o3=2-107.
DR PDB; 4U4Q; X-ray; 3.00 A; O3/o3=2-107.
DR PDB; 4U4R; X-ray; 2.80 A; O3/o3=2-107.
DR PDB; 4U4U; X-ray; 3.00 A; O3/o3=2-107.
DR PDB; 4U4Y; X-ray; 3.20 A; O3/o3=2-107.
DR PDB; 4U4Z; X-ray; 3.10 A; O3/o3=2-107.
DR PDB; 4U50; X-ray; 3.20 A; O3/o3=2-107.
DR PDB; 4U51; X-ray; 3.20 A; O3/o3=2-107.
DR PDB; 4U52; X-ray; 3.00 A; O3/o3=2-107.
DR PDB; 4U53; X-ray; 3.30 A; O3/o3=2-107.
DR PDB; 4U55; X-ray; 3.20 A; O3/o3=2-107.
DR PDB; 4U56; X-ray; 3.45 A; O3/o3=2-107.
DR PDB; 4U6F; X-ray; 3.10 A; O3/o3=2-107.
DR PDB; 4V6I; EM; 8.80 A; Bj=1-107.
DR PDB; 4V7F; EM; 8.70 A; e=1-107.
DR PDB; 4V88; X-ray; 3.00 A; Bf/Df=1-107.
DR PDB; 4V8T; EM; 8.10 A; f=1-107.
DR PDB; 4V8Y; EM; 4.30 A; Bf=2-107.
DR PDB; 4V8Z; EM; 6.60 A; Bf=2-107.
DR PDB; 4V91; EM; 3.70 A; f=1-107.
DR PDB; 5APN; EM; 3.91 A; f=1-107.
DR PDB; 5APO; EM; 3.41 A; f=1-107.
DR PDB; 5DAT; X-ray; 3.15 A; O3/o3=2-107.
DR PDB; 5DC3; X-ray; 3.25 A; O3/o3=2-107.
DR PDB; 5DGE; X-ray; 3.45 A; O3/o3=2-107.
DR PDB; 5DGF; X-ray; 3.30 A; O3/o3=2-107.
DR PDB; 5DGV; X-ray; 3.10 A; O3/o3=2-107.
DR PDB; 5FCI; X-ray; 3.40 A; O3/o3=2-107.
DR PDB; 5FCJ; X-ray; 3.10 A; O3/o3=2-107.
DR PDB; 5FL8; EM; 9.50 A; f=1-107.
DR PDB; 5GAK; EM; 3.88 A; h=1-107.
DR PDB; 5H4P; EM; 3.07 A; f=1-107.
DR PDB; 5I4L; X-ray; 3.10 A; O3/o3=2-107.
DR PDB; 5JCS; EM; 9.50 A; f=1-107.
DR PDB; 5JUO; EM; 4.00 A; KA=1-107.
DR PDB; 5JUP; EM; 3.50 A; KA=1-107.
DR PDB; 5JUS; EM; 4.20 A; KA=1-107.
DR PDB; 5JUT; EM; 4.00 A; KA=1-107.
DR PDB; 5JUU; EM; 4.00 A; KA=1-107.
DR PDB; 5LYB; X-ray; 3.25 A; O3/o3=2-107.
DR PDB; 5M1J; EM; 3.30 A; f5=2-107.
DR PDB; 5MC6; EM; 3.80 A; BK=1-107.
DR PDB; 5MEI; X-ray; 3.50 A; AG/DH=2-107.
DR PDB; 5NDG; X-ray; 3.70 A; O3/o3=2-107.
DR PDB; 5NDV; X-ray; 3.30 A; O3/o3=2-107.
DR PDB; 5NDW; X-ray; 3.70 A; O3/o3=2-107.
DR PDB; 5OBM; X-ray; 3.40 A; O3/o3=2-107.
DR PDB; 5ON6; X-ray; 3.10 A; AG/DH=2-107.
DR PDB; 5T62; EM; 3.30 A; s=1-107.
DR PDB; 5T6R; EM; 4.50 A; s=1-107.
DR PDB; 5TBW; X-ray; 3.00 A; AG/DH=2-107.
DR PDB; 5TGA; X-ray; 3.30 A; O3/o3=2-107.
DR PDB; 5TGM; X-ray; 3.50 A; O3/o3=2-107.
DR PDB; 5Z3G; EM; 3.65 A; j=1-107.
DR PDB; 6C0F; EM; 3.70 A; f=1-107.
DR PDB; 6CB1; EM; 4.60 A; f=1-107.
DR PDB; 6ELZ; EM; 3.30 A; f=1-107.
DR PDB; 6EM1; EM; 3.60 A; f=1-107.
DR PDB; 6EM3; EM; 3.20 A; f=1-107.
DR PDB; 6EM4; EM; 4.10 A; f=1-107.
DR PDB; 6EM5; EM; 4.30 A; f=1-107.
DR PDB; 6FT6; EM; 3.90 A; f=1-107.
DR PDB; 6GQ1; EM; 4.40 A; f=2-107.
DR PDB; 6GQB; EM; 3.90 A; f=2-107.
DR PDB; 6GQV; EM; 4.00 A; f=2-107.
DR PDB; 6HD7; EM; 3.40 A; h=1-107.
DR PDB; 6HHQ; X-ray; 3.10 A; AG/DH=1-107.
DR PDB; 6I7O; EM; 5.30 A; BK/YK=2-107.
DR PDB; 6M62; EM; 3.20 A; f=1-107.
DR PDB; 6N8J; EM; 3.50 A; f=1-107.
DR PDB; 6N8K; EM; 3.60 A; f=1-107.
DR PDB; 6N8L; EM; 3.60 A; f=1-107.
DR PDB; 6N8M; EM; 3.50 A; s=1-107.
DR PDB; 6N8N; EM; 3.80 A; s=1-107.
DR PDB; 6N8O; EM; 3.50 A; s=1-107.
DR PDB; 6OIG; EM; 3.80 A; f=2-107.
DR PDB; 6Q8Y; EM; 3.10 A; BK=2-107.
DR PDB; 6QIK; EM; 3.10 A; f=1-107.
DR PDB; 6QT0; EM; 3.40 A; f=1-107.
DR PDB; 6QTZ; EM; 3.50 A; f=1-107.
DR PDB; 6R84; EM; 3.60 A; h=2-107.
DR PDB; 6R86; EM; 3.40 A; h=2-107.
DR PDB; 6R87; EM; 3.40 A; h=2-107.
DR PDB; 6RI5; EM; 3.30 A; f=1-107.
DR PDB; 6RZZ; EM; 3.20 A; f=1-107.
DR PDB; 6S05; EM; 3.90 A; f=1-107.
DR PDB; 6S47; EM; 3.28 A; Ah=2-107.
DR PDB; 6SNT; EM; 2.80 A; ak=1-107.
DR PDB; 6SV4; EM; 3.30 A; BK/YK/ZK=1-107.
DR PDB; 6T4Q; EM; 2.60 A; Lf=2-107.
DR PDB; 6T7I; EM; 3.20 A; Lf=1-107.
DR PDB; 6T7T; EM; 3.10 A; Lf=1-107.
DR PDB; 6T83; EM; 4.00 A; Q/fy=1-107.
DR PDB; 6TB3; EM; 2.80 A; BK=2-107.
DR PDB; 6TNU; EM; 3.10 A; BK=2-107.
DR PDB; 6WOO; EM; 2.90 A; f=2-106.
DR PDB; 6XIQ; EM; 4.20 A; f=1-107.
DR PDB; 6XIR; EM; 3.20 A; f=1-107.
DR PDB; 6YLG; EM; 3.00 A; f=1-107.
DR PDB; 6YLH; EM; 3.10 A; f=1-107.
DR PDB; 6YLX; EM; 3.90 A; f=1-107.
DR PDB; 6YLY; EM; 3.80 A; f=1-107.
DR PDB; 6Z6J; EM; 3.40 A; Lf=1-107.
DR PDB; 6Z6K; EM; 3.40 A; Lf=1-107.
DR PDB; 7AZY; EM; 2.88 A; v=1-107.
DR PDB; 7B7D; EM; 3.30 A; Lb=2-107.
DR PDB; 7BT6; EM; 3.12 A; f=1-107.
DR PDB; 7BTB; EM; 3.22 A; f=1-107.
DR PDB; 7NRC; EM; 3.90 A; Lh=2-107.
DR PDB; 7NRD; EM; 4.36 A; Lh=2-107.
DR PDB; 7OF1; EM; 3.10 A; f=1-107.
DR PDB; 7OH3; EM; 3.40 A; f=1-107.
DR PDB; 7OHP; EM; 3.90 A; f=1-107.
DR PDB; 7OHQ; EM; 3.10 A; f=1-107.
DR PDB; 7OHR; EM; 4.72 A; f=1-107.
DR PDB; 7OHS; EM; 4.38 A; f=1-107.
DR PDB; 7OHT; EM; 4.70 A; f=1-107.
DR PDB; 7OHU; EM; 3.70 A; f=1-107.
DR PDB; 7OHV; EM; 3.90 A; f=1-107.
DR PDB; 7OHW; EM; 3.50 A; f=1-107.
DR PDB; 7OHX; EM; 3.30 A; f=1-107.
DR PDB; 7OHY; EM; 3.90 A; f=1-107.
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; 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; 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; 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 AlphaFoldDB; P05744; -.
DR SMR; P05744; -.
DR BioGRID; 36040; 149.
DR IntAct; P05744; 19.
DR MINT; P05744; -.
DR STRING; 4932.YPL143W; -.
DR iPTMnet; P05744; -.
DR MaxQB; P05744; -.
DR PaxDb; P05744; -.
DR PRIDE; P05744; -.
DR TopDownProteomics; P05744; -.
DR EnsemblFungi; YPL143W_mRNA; YPL143W; YPL143W.
DR GeneID; 855960; -.
DR KEGG; sce:YPL143W; -.
DR SGD; S000006064; RPL33A.
DR VEuPathDB; FungiDB:YPL143W; -.
DR eggNOG; KOG0887; Eukaryota.
DR GeneTree; ENSGT00390000016972; -.
DR HOGENOM; CLU_100745_2_0_1; -.
DR InParanoid; P05744; -.
DR OMA; FKRHGRL; -.
DR BioCyc; YEAST:G3O-34040-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:P05744; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P05744; 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:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR Gene3D; 2.40.10.190; -; 1.
DR HAMAP; MF_00573; Ribosomal_L35Ae; 1.
DR InterPro; IPR038661; L35A_sf.
DR InterPro; IPR001780; Ribosomal_L35A.
DR InterPro; IPR018266; Ribosomal_L35Ae_CS.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR10902; PTHR10902; 1.
DR Pfam; PF01247; Ribosomal_L35Ae; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR PROSITE; PS01105; RIBOSOMAL_L35AE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:18782943"
FT CHAIN 2..107
FT /note="60S ribosomal protein L33-A"
FT /id="PRO_0000192807"
FT MOD_RES 2
FT /note="N-acetylalanine; partial"
FT /evidence="ECO:0000269|PubMed:10601260"
FT CROSSLNK 47
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 24
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 8..18
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 63..74
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 107 AA; 12154 MW; 263E8389218B5027 CRC64;
MAESHRLYVK GKHLSYQRSK RVNNPNVSLI KIEGVATPQD AQFYLGKRIA YVYRASKEVR
GSKIRVMWGK VTRTHGNSGV VRATFRNNLP AKTFGASVRI FLYPSNI
