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RL37A_YEAST
ID   RL37A_YEAST             Reviewed;          88 AA.
AC   P49166; D6VYI8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 175.
DE   RecName: Full=60S ribosomal protein L37-A {ECO:0000303|PubMed:9559554};
DE   AltName: Full=L43;
DE   AltName: Full=Large ribosomal subunit protein eL37-A {ECO:0000303|PubMed:24524803};
DE   AltName: Full=YL35;
DE   AltName: Full=YP55;
GN   Name=RPL37A {ECO:0000303|PubMed:9559554}; Synonyms=RPL35A;
GN   OrderedLocusNames=YLR185W; ORFNames=L9470.6;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
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   PROTEIN SEQUENCE OF 2-88.
RA   Itoh T., Higo K., Otaka E., Osawa S.;
RT   "Studies on the primary structures of yeast ribosomal proteins.";
RL   (In) Osawa S., Ozeki H., Uchida H., Yura T. (eds.);
RL   Genetics and evolution of RNA polymerase, tRNA and ribosomes, pp.609-624,
RL   University of Tokyo Press, Tokyo (1980).
RN   [4]
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   [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   3D-STRUCTURE MODELING OF 2-53, 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   [9]
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   [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, SUBCELLULAR
RP   LOCATION, AND ZINC-BINDING.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:22096102};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|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 21800 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for eL37 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL37 family.
CC       {ECO:0000305}.
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DR   EMBL; U17246; AAB67458.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09504.1; -; Genomic_DNA.
DR   PIR; S51430; S51430.
DR   RefSeq; NP_013286.1; NM_001182072.1.
DR   PDB; 3J6X; EM; 6.10 A; 77=1-88.
DR   PDB; 3J6Y; EM; 6.10 A; 77=1-88.
DR   PDB; 3J77; EM; 6.20 A; 87=1-88.
DR   PDB; 3J78; EM; 6.30 A; 87=1-88.
DR   PDB; 3JCT; EM; 3.08 A; j=1-88.
DR   PDB; 4U3M; X-ray; 3.00 A; O7/o7=2-88.
DR   PDB; 4U3N; X-ray; 3.20 A; O7/o7=2-88.
DR   PDB; 4U3U; X-ray; 2.90 A; O7/o7=2-88.
DR   PDB; 4U4N; X-ray; 3.10 A; O7/o7=2-88.
DR   PDB; 4U4O; X-ray; 3.60 A; O7/o7=2-88.
DR   PDB; 4U4Q; X-ray; 3.00 A; O7/o7=2-88.
DR   PDB; 4U4R; X-ray; 2.80 A; O7/o7=2-88.
DR   PDB; 4U4U; X-ray; 3.00 A; O7/o7=2-88.
DR   PDB; 4U4Y; X-ray; 3.20 A; O7/o7=2-88.
DR   PDB; 4U4Z; X-ray; 3.10 A; O7/o7=2-88.
DR   PDB; 4U50; X-ray; 3.20 A; O7/o7=2-88.
DR   PDB; 4U51; X-ray; 3.20 A; O7/o7=2-88.
DR   PDB; 4U52; X-ray; 3.00 A; O7/o7=2-88.
DR   PDB; 4U53; X-ray; 3.30 A; O7/o7=2-88.
DR   PDB; 4U55; X-ray; 3.20 A; O7/o7=2-88.
DR   PDB; 4U56; X-ray; 3.45 A; O7/o7=2-88.
DR   PDB; 4U6F; X-ray; 3.10 A; O7/o7=2-88.
DR   PDB; 4V4B; EM; 11.70 A; BY=2-88.
DR   PDB; 4V6I; EM; 8.80 A; Bl=1-88.
DR   PDB; 4V7F; EM; 8.70 A; h=1-88.
DR   PDB; 4V7R; X-ray; 4.00 A; Bd/Dd=1-88.
DR   PDB; 4V88; X-ray; 3.00 A; Bj/Dj=1-88.
DR   PDB; 4V8T; EM; 8.10 A; j=1-88.
DR   PDB; 4V8Y; EM; 4.30 A; Bj=2-88.
DR   PDB; 4V8Z; EM; 6.60 A; Bj=2-88.
DR   PDB; 4V91; EM; 3.70 A; j=1-88.
DR   PDB; 5APN; EM; 3.91 A; j=1-88.
DR   PDB; 5APO; EM; 3.41 A; j=1-88.
DR   PDB; 5DAT; X-ray; 3.15 A; O7/o7=2-88.
DR   PDB; 5DC3; X-ray; 3.25 A; O7/o7=2-88.
DR   PDB; 5DGE; X-ray; 3.45 A; O7/o7=2-88.
DR   PDB; 5DGF; X-ray; 3.30 A; O7/o7=2-88.
DR   PDB; 5DGV; X-ray; 3.10 A; O7/o7=2-88.
DR   PDB; 5FCI; X-ray; 3.40 A; O7/o7=2-88.
DR   PDB; 5FCJ; X-ray; 3.10 A; O7/o7=2-88.
DR   PDB; 5FL8; EM; 9.50 A; j=1-88.
DR   PDB; 5GAK; EM; 3.88 A; l=1-88.
DR   PDB; 5H4P; EM; 3.07 A; j=1-88.
DR   PDB; 5I4L; X-ray; 3.10 A; O7/o7=2-88.
DR   PDB; 5JCS; EM; 9.50 A; j=1-88.
DR   PDB; 5JUO; EM; 4.00 A; OA=1-88.
DR   PDB; 5JUP; EM; 3.50 A; OA=1-88.
DR   PDB; 5JUS; EM; 4.20 A; OA=1-88.
DR   PDB; 5JUT; EM; 4.00 A; OA=1-88.
DR   PDB; 5JUU; EM; 4.00 A; OA=1-88.
DR   PDB; 5LYB; X-ray; 3.25 A; O7/o7=2-88.
DR   PDB; 5M1J; EM; 3.30 A; j5=2-88.
DR   PDB; 5MC6; EM; 3.80 A; AF=1-88.
DR   PDB; 5MEI; X-ray; 3.50 A; AK/DL=2-88.
DR   PDB; 5NDG; X-ray; 3.70 A; O7/o7=2-85.
DR   PDB; 5NDV; X-ray; 3.30 A; O7/o7=2-88.
DR   PDB; 5NDW; X-ray; 3.70 A; O7/o7=2-88.
DR   PDB; 5OBM; X-ray; 3.40 A; O7/o7=2-88.
DR   PDB; 5ON6; X-ray; 3.10 A; AK/DL=2-88.
DR   PDB; 5T62; EM; 3.30 A; w=1-88.
DR   PDB; 5T6R; EM; 4.50 A; w=1-88.
DR   PDB; 5TBW; X-ray; 3.00 A; AK/DL=2-88.
DR   PDB; 5TGA; X-ray; 3.30 A; O7/o7=2-88.
DR   PDB; 5TGM; X-ray; 3.50 A; O7/o7=2-88.
DR   PDB; 5Z3G; EM; 3.65 A; n=1-88.
DR   PDB; 6C0F; EM; 3.70 A; j=1-88.
DR   PDB; 6CB1; EM; 4.60 A; j=1-88.
DR   PDB; 6ELZ; EM; 3.30 A; j=1-88.
DR   PDB; 6EM1; EM; 3.60 A; j=1-88.
DR   PDB; 6EM3; EM; 3.20 A; j=1-88.
DR   PDB; 6EM4; EM; 4.10 A; j=1-88.
DR   PDB; 6EM5; EM; 4.30 A; j=1-88.
DR   PDB; 6FT6; EM; 3.90 A; j=1-88.
DR   PDB; 6GQ1; EM; 4.40 A; j=2-88.
DR   PDB; 6GQB; EM; 3.90 A; j=2-88.
DR   PDB; 6GQV; EM; 4.00 A; j=2-88.
DR   PDB; 6HD7; EM; 3.40 A; l=1-88.
DR   PDB; 6HHQ; X-ray; 3.10 A; AK/DL=1-88.
DR   PDB; 6I7O; EM; 5.30 A; AF/XF=2-83.
DR   PDB; 6M62; EM; 3.20 A; j=1-88.
DR   PDB; 6N8J; EM; 3.50 A; j=1-88.
DR   PDB; 6N8K; EM; 3.60 A; j=1-88.
DR   PDB; 6N8L; EM; 3.60 A; j=1-88.
DR   PDB; 6N8M; EM; 3.50 A; w=1-88.
DR   PDB; 6N8N; EM; 3.80 A; w=1-88.
DR   PDB; 6N8O; EM; 3.50 A; w=1-88.
DR   PDB; 6OIG; EM; 3.80 A; j=2-88.
DR   PDB; 6Q8Y; EM; 3.10 A; AF=2-88.
DR   PDB; 6QIK; EM; 3.10 A; i=1-88.
DR   PDB; 6QT0; EM; 3.40 A; i=1-88.
DR   PDB; 6QTZ; EM; 3.50 A; i=1-88.
DR   PDB; 6R84; EM; 3.60 A; l=2-88.
DR   PDB; 6R86; EM; 3.40 A; l=2-88.
DR   PDB; 6R87; EM; 3.40 A; l=2-88.
DR   PDB; 6RI5; EM; 3.30 A; i=1-88.
DR   PDB; 6RZZ; EM; 3.20 A; i=1-88.
DR   PDB; 6S05; EM; 3.90 A; i=1-88.
DR   PDB; 6S47; EM; 3.28 A; Al=2-88.
DR   PDB; 6SNT; EM; 2.80 A; ag=1-88.
DR   PDB; 6SV4; EM; 3.30 A; AF/XF/zF=1-88.
DR   PDB; 6T4Q; EM; 2.60 A; Lj=2-86.
DR   PDB; 6T7I; EM; 3.20 A; Lj=1-88.
DR   PDB; 6T7T; EM; 3.10 A; Lj=1-88.
DR   PDB; 6T83; EM; 4.00 A; U/jb=1-88.
DR   PDB; 6TB3; EM; 2.80 A; AF=2-82.
DR   PDB; 6TNU; EM; 3.10 A; AF=2-82.
DR   PDB; 6WOO; EM; 2.90 A; j=2-83.
DR   PDB; 6XIQ; EM; 4.20 A; j=1-88.
DR   PDB; 6XIR; EM; 3.20 A; j=1-88.
DR   PDB; 6YLG; EM; 3.00 A; j=1-88.
DR   PDB; 6YLH; EM; 3.10 A; j=1-88.
DR   PDB; 6YLX; EM; 3.90 A; j=1-88.
DR   PDB; 6YLY; EM; 3.80 A; j=1-88.
DR   PDB; 6Z6J; EM; 3.40 A; Lj=1-88.
DR   PDB; 6Z6K; EM; 3.40 A; Lj=1-88.
DR   PDB; 7AZY; EM; 2.88 A; g=1-88.
DR   PDB; 7B7D; EM; 3.30 A; Lf=2-82.
DR   PDB; 7BT6; EM; 3.12 A; j=1-88.
DR   PDB; 7BTB; EM; 3.22 A; j=1-88.
DR   PDB; 7NRC; EM; 3.90 A; Ll=2-82.
DR   PDB; 7NRD; EM; 4.36 A; Ll=2-82.
DR   PDB; 7OF1; EM; 3.10 A; j=1-88.
DR   PDB; 7OH3; EM; 3.40 A; j=1-88.
DR   PDB; 7OHP; EM; 3.90 A; j=1-88.
DR   PDB; 7OHQ; EM; 3.10 A; j=1-88.
DR   PDB; 7OHR; EM; 4.72 A; j=1-88.
DR   PDB; 7OHS; EM; 4.38 A; j=1-88.
DR   PDB; 7OHU; EM; 3.70 A; j=1-88.
DR   PDB; 7OHV; EM; 3.90 A; j=1-88.
DR   PDB; 7OHW; EM; 3.50 A; j=1-88.
DR   PDB; 7OHX; EM; 3.30 A; j=1-88.
DR   PDB; 7OHY; EM; 3.90 A; j=1-88.
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; 7OHU; -.
DR   PDBsum; 7OHV; -.
DR   PDBsum; 7OHW; -.
DR   PDBsum; 7OHX; -.
DR   PDBsum; 7OHY; -.
DR   AlphaFoldDB; P49166; -.
DR   SMR; P49166; -.
DR   BioGRID; 31455; 254.
DR   DIP; DIP-2135N; -.
DR   IntAct; P49166; 5.
DR   MINT; P49166; -.
DR   STRING; 4932.YLR185W; -.
DR   CarbonylDB; P49166; -.
DR   iPTMnet; P49166; -.
DR   MaxQB; P49166; -.
DR   PaxDb; P49166; -.
DR   PRIDE; P49166; -.
DR   EnsemblFungi; YLR185W_mRNA; YLR185W; YLR185W.
DR   GeneID; 850882; -.
DR   KEGG; sce:YLR185W; -.
DR   SGD; S000004175; RPL37A.
DR   VEuPathDB; FungiDB:YLR185W; -.
DR   eggNOG; KOG3475; Eukaryota.
DR   GeneTree; ENSGT00940000168926; -.
DR   HOGENOM; CLU_150908_2_1_1; -.
DR   InParanoid; P49166; -.
DR   OMA; RMAYLKH; -.
DR   BioCyc; YEAST:G3O-32308-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; P49166; -.
DR   PRO; PR:P49166; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P49166; protein.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IC:SGD.
DR   GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD.
DR   GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR   Gene3D; 2.20.25.30; -; 1.
DR   HAMAP; MF_00547; Ribosomal_L37e; 1.
DR   InterPro; IPR011331; Ribosomal_L37ae/L37e.
DR   InterPro; IPR001569; Ribosomal_L37e.
DR   InterPro; IPR018267; Ribosomal_L37e_CS.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   Pfam; PF01907; Ribosomal_L37e; 1.
DR   SUPFAM; SSF57829; SSF57829; 1.
DR   PROSITE; PS01077; RIBOSOMAL_L37E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Metal-binding;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.3"
FT   CHAIN           2..88
FT                   /note="60S ribosomal protein L37-A"
FT                   /id="PRO_0000139722"
FT   ZN_FING         19..37
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:22096102"
FT   BINDING         22
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:22096102"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:22096102"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:22096102"
FT   CONFLICT        73
FT                   /note="R -> RR (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   TURN            20..22
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   TURN            29..32
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           51..56
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:6EM3"
FT   HELIX           70..76
FT                   /evidence="ECO:0007829|PDB:6EM3"
SQ   SEQUENCE   88 AA;  9850 MW;  274D249361EBE5E5 CRC64;
     MGKGTPSFGK RHNKSHTLCN RCGRRSFHVQ KKTCSSCGYP AAKTRSYNWG AKAKRRHTTG
     TGRMRYLKHV SRRFKNGFQT GSASKASA
 
 
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