RL7A_YEAST
ID RL7A_YEAST Reviewed; 244 AA.
AC P05737; D6VU68; P87029;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=60S ribosomal protein L7-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L6;
DE AltName: Full=Large ribosomal subunit protein uL30-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=RP11;
DE AltName: Full=YL8;
GN Name=RPL7A {ECO:0000303|PubMed:9559554}; Synonyms=RPL6A, RPL8A, YL8A;
GN OrderedLocusNames=YGL076C;
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=1549461; DOI=10.1093/nar/20.5.1011;
RA Mizuta K., Hashimoto T., Otaka E.;
RT "Yeast ribosomal proteins: XIII. Saccharomyces cerevisiae YL8A gene,
RT interrupted with two introns, encodes a homolog of mammalian L7.";
RL Nucleic Acids Res. 20:1011-1016(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(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 2-41, 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 PROTEIN SEQUENCE OF 2-21.
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 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 [8]
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 [9]
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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 83-243, 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 83-244, 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 101000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uL30 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL30 family.
CC {ECO:0000305}.
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DR EMBL; X62627; CAA44495.1; -; Genomic_DNA.
DR EMBL; Z72598; CAA96781.1; -; Genomic_DNA.
DR EMBL; Z72597; CAA96779.2; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006941; DAA08029.1; -; Genomic_DNA.
DR PIR; S22789; R5BYL7.
DR RefSeq; NP_011439.1; NM_001180941.1.
DR PDB; 3J6X; EM; 6.10 A; L7=1-244.
DR PDB; 3J6Y; EM; 6.10 A; L7=1-244.
DR PDB; 3J77; EM; 6.20 A; L7=1-244.
DR PDB; 3J78; EM; 6.30 A; L7=1-244.
DR PDB; 3JCT; EM; 3.08 A; F=1-244.
DR PDB; 4U3M; X-ray; 3.00 A; L7/l7=2-244.
DR PDB; 4U3N; X-ray; 3.20 A; L7/l7=2-244.
DR PDB; 4U3U; X-ray; 2.90 A; L7/l7=2-244.
DR PDB; 4U4N; X-ray; 3.10 A; L7/l7=2-244.
DR PDB; 4U4O; X-ray; 3.60 A; L7/l7=2-244.
DR PDB; 4U4Q; X-ray; 3.00 A; L7/l7=2-244.
DR PDB; 4U4R; X-ray; 2.80 A; L7/l7=2-244.
DR PDB; 4U4U; X-ray; 3.00 A; L7/l7=2-244.
DR PDB; 4U4Y; X-ray; 3.20 A; L7/l7=2-244.
DR PDB; 4U4Z; X-ray; 3.10 A; L7/l7=2-244.
DR PDB; 4U50; X-ray; 3.20 A; L7/l7=2-244.
DR PDB; 4U51; X-ray; 3.20 A; L7/l7=2-244.
DR PDB; 4U52; X-ray; 3.00 A; L7/l7=2-244.
DR PDB; 4U53; X-ray; 3.30 A; L7/l7=2-244.
DR PDB; 4U55; X-ray; 3.20 A; L7/l7=2-244.
DR PDB; 4U56; X-ray; 3.45 A; L7/l7=2-244.
DR PDB; 4U6F; X-ray; 3.10 A; L7/l7=2-244.
DR PDB; 4V4B; EM; 11.70 A; BF=83-244.
DR PDB; 4V6I; EM; 8.80 A; Be=1-244.
DR PDB; 4V7F; EM; 8.70 A; a=1-244.
DR PDB; 4V7R; X-ray; 4.00 A; BG/DG=1-244.
DR PDB; 4V88; X-ray; 3.00 A; BF/DF=1-244.
DR PDB; 4V8T; EM; 8.10 A; F=1-244.
DR PDB; 4V8Y; EM; 4.30 A; BF=2-244.
DR PDB; 4V8Z; EM; 6.60 A; BF=2-244.
DR PDB; 4V91; EM; 3.70 A; F=1-244.
DR PDB; 5APN; EM; 3.91 A; F=1-244.
DR PDB; 5APO; EM; 3.41 A; F=1-244.
DR PDB; 5DAT; X-ray; 3.15 A; L7/l7=2-244.
DR PDB; 5DC3; X-ray; 3.25 A; L7/l7=2-244.
DR PDB; 5DGE; X-ray; 3.45 A; L7/l7=2-244.
DR PDB; 5DGF; X-ray; 3.30 A; L7/l7=2-244.
DR PDB; 5DGV; X-ray; 3.10 A; L7/l7=2-244.
DR PDB; 5FCI; X-ray; 3.40 A; L7/l7=2-244.
DR PDB; 5FCJ; X-ray; 3.10 A; L7/l7=2-244.
DR PDB; 5FL8; EM; 9.50 A; F=1-244.
DR PDB; 5GAK; EM; 3.88 A; J=1-244.
DR PDB; 5H4P; EM; 3.07 A; F=1-244.
DR PDB; 5I4L; X-ray; 3.10 A; L7/l7=22-244.
DR PDB; 5JCS; EM; 9.50 A; F=1-244.
DR PDB; 5JUO; EM; 4.00 A; K=1-244.
DR PDB; 5JUP; EM; 3.50 A; K=1-244.
DR PDB; 5JUS; EM; 4.20 A; K=1-244.
DR PDB; 5JUT; EM; 4.00 A; K=1-244.
DR PDB; 5JUU; EM; 4.00 A; K=1-244.
DR PDB; 5LYB; X-ray; 3.25 A; L7/l7=22-244.
DR PDB; 5M1J; EM; 3.30 A; F5=23-244.
DR PDB; 5MC6; EM; 3.80 A; BO=1-244.
DR PDB; 5MEI; X-ray; 3.50 A; CI/o=23-244.
DR PDB; 5NDG; X-ray; 3.70 A; L7/l7=22-244.
DR PDB; 5NDV; X-ray; 3.30 A; L7/l7=19-244.
DR PDB; 5NDW; X-ray; 3.70 A; L7/l7=22-244.
DR PDB; 5OBM; X-ray; 3.40 A; L7/l7=22-244.
DR PDB; 5ON6; X-ray; 3.10 A; CI/o=23-244.
DR PDB; 5T62; EM; 3.30 A; I=1-244.
DR PDB; 5T6R; EM; 4.50 A; I=1-244.
DR PDB; 5TBW; X-ray; 3.00 A; CI/o=23-244.
DR PDB; 5TGA; X-ray; 3.30 A; L7/l7=22-244.
DR PDB; 5TGM; X-ray; 3.50 A; L7/l7=22-244.
DR PDB; 5Z3G; EM; 3.65 A; J=1-244.
DR PDB; 6C0F; EM; 3.70 A; F=1-244.
DR PDB; 6CB1; EM; 4.60 A; F=1-244.
DR PDB; 6ELZ; EM; 3.30 A; F=1-244.
DR PDB; 6EM1; EM; 3.60 A; F=1-244.
DR PDB; 6EM3; EM; 3.20 A; F=1-244.
DR PDB; 6EM4; EM; 4.10 A; F=1-244.
DR PDB; 6EM5; EM; 4.30 A; F=1-244.
DR PDB; 6FT6; EM; 3.90 A; F=1-244.
DR PDB; 6GQ1; EM; 4.40 A; F=23-244.
DR PDB; 6GQB; EM; 3.90 A; F=23-244.
DR PDB; 6GQV; EM; 4.00 A; F=23-244.
DR PDB; 6HD7; EM; 3.40 A; J=1-244.
DR PDB; 6HHQ; X-ray; 3.10 A; CI/o=1-244.
DR PDB; 6I7O; EM; 5.30 A; BO/YO=22-244.
DR PDB; 6M62; EM; 3.20 A; F=1-244.
DR PDB; 6N8J; EM; 3.50 A; F=1-244.
DR PDB; 6N8K; EM; 3.60 A; F=1-244.
DR PDB; 6N8L; EM; 3.60 A; F=1-244.
DR PDB; 6N8M; EM; 3.50 A; I=1-244.
DR PDB; 6N8N; EM; 3.80 A; I=1-244.
DR PDB; 6N8O; EM; 3.50 A; I=1-244.
DR PDB; 6OIG; EM; 3.80 A; F=23-244.
DR PDB; 6Q8Y; EM; 3.10 A; BO=23-244.
DR PDB; 6QIK; EM; 3.10 A; b=1-244.
DR PDB; 6QT0; EM; 3.40 A; b=1-244.
DR PDB; 6QTZ; EM; 3.50 A; b=1-244.
DR PDB; 6R84; EM; 3.60 A; J=23-244.
DR PDB; 6R86; EM; 3.40 A; J=23-244.
DR PDB; 6R87; EM; 3.40 A; J=23-244.
DR PDB; 6RI5; EM; 3.30 A; b=1-244.
DR PDB; 6RZZ; EM; 3.20 A; b=1-244.
DR PDB; 6S05; EM; 3.90 A; b=1-244.
DR PDB; 6S47; EM; 3.28 A; AI=2-244.
DR PDB; 6SNT; EM; 2.80 A; m=1-244.
DR PDB; 6SV4; EM; 3.30 A; BO/YO/ZO=1-244.
DR PDB; 6T4Q; EM; 2.60 A; LF=23-244.
DR PDB; 6T7I; EM; 3.20 A; LF=1-244.
DR PDB; 6T7T; EM; 3.10 A; LF=1-244.
DR PDB; 6T83; EM; 4.00 A; Fy/Ia=1-244.
DR PDB; 6TB3; EM; 2.80 A; BO=23-244.
DR PDB; 6TNU; EM; 3.10 A; BO=23-244.
DR PDB; 6WOO; EM; 2.90 A; F=23-244.
DR PDB; 6XIQ; EM; 4.20 A; F=1-244.
DR PDB; 6XIR; EM; 3.20 A; F=1-244.
DR PDB; 6YLG; EM; 3.00 A; F=1-244.
DR PDB; 6YLH; EM; 3.10 A; F=1-244.
DR PDB; 6YLX; EM; 3.90 A; F=1-244.
DR PDB; 6YLY; EM; 3.80 A; F=1-244.
DR PDB; 6Z6J; EM; 3.40 A; LF=1-244.
DR PDB; 6Z6K; EM; 3.40 A; LF=1-244.
DR PDB; 7AZY; EM; 2.88 A; C=1-244.
DR PDB; 7B7D; EM; 3.30 A; LI=23-244.
DR PDB; 7BT6; EM; 3.12 A; F=1-244.
DR PDB; 7BTB; EM; 3.22 A; F=1-244.
DR PDB; 7NRC; EM; 3.90 A; LI=23-244.
DR PDB; 7NRD; EM; 4.36 A; LI=23-244.
DR PDB; 7OF1; EM; 3.10 A; F=1-244.
DR PDB; 7OH3; EM; 3.40 A; F=1-244.
DR PDB; 7OHP; EM; 3.90 A; F=1-244.
DR PDB; 7OHQ; EM; 3.10 A; F=1-244.
DR PDB; 7OHR; EM; 4.72 A; F=1-244.
DR PDB; 7OHS; EM; 4.38 A; F=1-244.
DR PDB; 7OHT; EM; 4.70 A; F=1-244.
DR PDB; 7OHU; EM; 3.70 A; F=1-244.
DR PDB; 7OHV; EM; 3.90 A; F=1-244.
DR PDB; 7OHW; EM; 3.50 A; F=1-244.
DR PDB; 7OHX; EM; 3.30 A; F=1-244.
DR PDB; 7OHY; EM; 3.90 A; F=1-244.
DR PDB; 7OSA; X-ray; 3.00 A; uL30=1-244.
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; 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 PDBsum; 7OSA; -.
DR AlphaFoldDB; P05737; -.
DR SMR; P05737; -.
DR BioGRID; 33174; 121.
DR DIP; DIP-7124N; -.
DR IntAct; P05737; 134.
DR MINT; P05737; -.
DR STRING; 4932.YGL076C; -.
DR CarbonylDB; P05737; -.
DR iPTMnet; P05737; -.
DR MaxQB; P05737; -.
DR PaxDb; P05737; -.
DR PRIDE; P05737; -.
DR TopDownProteomics; P05737; -.
DR EnsemblFungi; YGL076C_mRNA; YGL076C; YGL076C.
DR GeneID; 852804; -.
DR KEGG; sce:YGL076C; -.
DR SGD; S000003044; RPL7A.
DR VEuPathDB; FungiDB:YGL076C; -.
DR eggNOG; KOG3184; Eukaryota.
DR GeneTree; ENSGT00950000182878; -.
DR HOGENOM; CLU_055156_0_2_1; -.
DR InParanoid; P05737; -.
DR OMA; SYYVDAQ; -.
DR BioCyc; YEAST:G3O-30577-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; P05737; -.
DR PRO; PR:P05737; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P05737; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:SGD.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IMP:SGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:SGD.
DR CDD; cd01657; Ribosomal_L7_archeal_euk; 1.
DR Gene3D; 3.30.1390.20; -; 2.
DR InterPro; IPR036919; L30_ferredoxin-like_sf.
DR InterPro; IPR018038; Ribosomal_L30_CS.
DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like.
DR InterPro; IPR012988; Ribosomal_L30_N.
DR InterPro; IPR039699; Ribosomal_L7/L30.
DR InterPro; IPR005998; Ribosomal_L7_euk.
DR InterPro; IPR035808; Ribosomal_L7_euk_arc.
DR PANTHER; PTHR11524; PTHR11524; 1.
DR Pfam; PF00327; Ribosomal_L30; 1.
DR Pfam; PF08079; Ribosomal_L30_N; 1.
DR SUPFAM; SSF55129; SSF55129; 1.
DR TIGRFAMs; TIGR01310; uL30_euk; 1.
DR PROSITE; PS00634; RIBOSOMAL_L30; 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, ECO:0000269|PubMed:18782943"
FT CHAIN 2..244
FT /note="60S ribosomal protein L7-A"
FT /id="PRO_0000104651"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 12..72
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 244 AA; 27638 MW; F65B24D48459F745 CRC64;
MAAEKILTPE SQLKKSKAQQ KTAEQVAAER AARKAANKEK RAIILERNAA YQKEYETAER
NIIQAKRDAK AAGSYYVEAQ HKLVFVVRIK GINKIPPKPR KVLQLLRLTR INSGTFVKVT
KATLELLKLI EPYVAYGYPS YSTIRQLVYK RGFGKINKQR VPLSDNAIIE ANLGKYGILS
IDDLIHEIIT VGPHFKQANN FLWPFKLSNP SGGWGVPRKF KHFIQGGSFG NREEFINKLV
KSMN
