ID RL25_YEAST Reviewed; 142 AA. AC P04456; D6W1U1; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 02-SEP-2026, entry version 225. DE RecName: Full=Large ribosomal subunit protein uL23 {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L25 {ECO:0000303|PubMed:9559554}; DE AltName: Full=RP16L; DE AltName: Full=YL25; DE AltName: Full=YP42'; GN Name=RPL25 {ECO:0000303|PubMed:9559554}; OrderedLocusNames=YOL127W; 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; RX PubMed=6091033; DOI=10.1093/nar/12.17.6685; RA Leer R.J., van Raamsdonk-Duin M.M.C., Hagendoorn M.J.M., Mager W.H., RA Planta R.J.; RT "Structural comparison of yeast ribosomal protein genes."; RL Nucleic Acids Res. 12:6685-6700(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8896265; RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1013::aid-yea980%3e3.0.co;2-5; RA Casamayor A., Khalid H., Balcells L., Aldea M., Casas C., Herrero E., RA Arino J.; RT "Sequence analysis of a 13.4 kbp fragment from the left arm of chromosome RT XV reveals a malate dehydrogenase gene, a putative Ser/Thr protein kinase, RT the ribosomal L25 gene and four new open reading frames."; RL Yeast 12:1013-1020(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; DOI=10.1038/387s098; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(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 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 [6] 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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [10] 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 [11] RP IDENTIFICATION BY MASS 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 [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 60-136, 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 60-142, 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-61, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=EJY251-11b; RX PubMed=15542864; DOI=10.1074/mcp.m400154-mcp200; RA Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D., RA Gygi S.P.; RT "A proteomic strategy for gaining insights into protein sumoylation in RT yeast."; RL Mol. Cell. Proteomics 4:246-254(2005). RN [16] 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 [17] 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. uL23 is a major component of the universal docking site for CC these factors at the polypeptide exit tunnel. CC {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). uL23 is associated with the polypeptide CC exit tunnel (PubMed:22096102, PubMed:9559554). CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}. CC -!- INTERACTION: CC P04456; P38861: NMD3; NbExp=2; IntAct=EBI-15308, EBI-12077; CC P04456; Q01560: NPL3; NbExp=2; IntAct=EBI-15308, EBI-12114; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 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; U41293; AAC49465.1; -; Genomic_DNA. DR EMBL; X01014; CAA25506.1; -; Genomic_DNA. DR EMBL; Z74869; CAA99146.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10657.1; -; Genomic_DNA. DR PIR; S63443; R5BY25. DR RefSeq; NP_014514.1; NM_001183381.1. DR PDB; 2WW9; EM; 8.60 A; K=1-142. DR PDB; 2WWA; EM; 8.90 A; K=1-142. DR PDB; 2WWB; EM; 6.48 A; K=1-142. DR PDB; 3J6X; EM; 6.10 A; 65=1-142. DR PDB; 3J6Y; EM; 6.10 A; 65=1-142. DR PDB; 3J77; EM; 6.20 A; 75=1-142. DR PDB; 3J78; EM; 6.30 A; 75=1-142. DR PDB; 3JCT; EM; 3.08 A; X=1-142. DR PDB; 4U3M; X-ray; 3.00 A; N5/n5=2-142. DR PDB; 4U3N; X-ray; 3.20 A; N5/n5=2-142. DR PDB; 4U3U; X-ray; 2.90 A; N5/n5=2-142. DR PDB; 4U4N; X-ray; 3.10 A; N5/n5=2-142. DR PDB; 4U4O; X-ray; 3.60 A; N5/n5=2-142. DR PDB; 4U4Q; X-ray; 3.00 A; N5/n5=2-142. DR PDB; 4U4R; X-ray; 2.80 A; N5/n5=2-142. DR PDB; 4U4U; X-ray; 3.00 A; N5/n5=2-142. DR PDB; 4U4Y; X-ray; 3.20 A; N5/n5=2-142. DR PDB; 4U4Z; X-ray; 3.10 A; N5/n5=2-142. DR PDB; 4U50; X-ray; 3.20 A; N5/n5=2-142. DR PDB; 4U51; X-ray; 3.20 A; N5/n5=2-142. DR PDB; 4U52; X-ray; 3.00 A; N5/n5=2-142. DR PDB; 4U53; X-ray; 3.30 A; N5/n5=2-142. DR PDB; 4U55; X-ray; 3.20 A; N5/n5=2-142. DR PDB; 4U56; X-ray; 3.45 A; N5/n5=2-142. DR PDB; 4U6F; X-ray; 3.10 A; N5/n5=2-142. DR PDB; 4V4B; EM; 11.70 A; BT=60-142. DR PDB; 4V5Z; EM; 8.70 A; Bs=4-142. DR PDB; 4V6I; EM; 8.80 A; BX=1-142. DR PDB; 4V7F; EM; 8.70 A; W=1-142. DR PDB; 4V7R; X-ray; 4.00 A; BW/DW=1-142. DR PDB; 4V88; X-ray; 3.00 A; BX/DX=1-142. DR PDB; 4V8T; EM; 8.10 A; X=1-142. DR PDB; 4V8Y; EM; 4.30 A; BX=2-142. DR PDB; 4V8Z; EM; 6.60 A; BX=2-142. DR PDB; 4V91; EM; 3.70 A; X=1-142. DR PDB; 5APN; EM; 3.91 A; X=1-142. DR PDB; 5APO; EM; 3.41 A; X=1-142. DR PDB; 5DAT; X-ray; 3.15 A; N5/n5=2-142. DR PDB; 5DC3; X-ray; 3.25 A; N5/n5=2-142. DR PDB; 5DGE; X-ray; 3.45 A; N5/n5=2-142. DR PDB; 5DGF; X-ray; 3.30 A; N5/n5=2-142. DR PDB; 5DGV; X-ray; 3.10 A; N5/n5=2-142. DR PDB; 5FCI; X-ray; 3.40 A; N5/n5=2-142. DR PDB; 5FCJ; X-ray; 3.10 A; N5/n5=2-142. DR PDB; 5GAK; EM; 3.88 A; Z=1-142. DR PDB; 5H4P; EM; 3.07 A; X=1-142. DR PDB; 5I4L; X-ray; 3.10 A; N5/n5=22-142. DR PDB; 5JCS; EM; 9.50 A; X=1-142. DR PDB; 5JUO; EM; 4.00 A; CA=1-142. DR PDB; 5JUP; EM; 3.50 A; CA=1-142. DR PDB; 5JUS; EM; 4.20 A; CA=1-142. DR PDB; 5JUT; EM; 4.00 A; CA=1-142. DR PDB; 5JUU; EM; 4.00 A; CA=1-142. DR PDB; 5LYB; X-ray; 3.25 A; N5/n5=22-142. DR PDB; 5M1J; EM; 3.30 A; X5=22-142. DR PDB; 5MC6; EM; 3.80 A; AH=1-142. DR PDB; 5MEI; X-ray; 3.50 A; 8/CZ=22-142. DR PDB; 5NDG; X-ray; 3.70 A; N5/n5=22-142. DR PDB; 5NDV; X-ray; 3.30 A; N5/n5=23-142. DR PDB; 5NDW; X-ray; 3.70 A; N5/n5=22-142. DR PDB; 5OBM; X-ray; 3.40 A; N5/n5=22-142. DR PDB; 5ON6; X-ray; 3.10 A; 8/CZ=22-142. DR PDB; 5T62; EM; 3.30 A; k=1-142. DR PDB; 5T6R; EM; 4.50 A; k=1-142. DR PDB; 5TBW; X-ray; 3.00 A; 8/CZ=22-142. DR PDB; 5TGA; X-ray; 3.30 A; N5/n5=22-142. DR PDB; 5TGM; X-ray; 3.50 A; N5/n5=22-142. DR PDB; 6CB1; EM; 4.60 A; X=1-142. DR PDB; 6ELZ; EM; 3.30 A; X=1-142. DR PDB; 6EM5; EM; 4.30 A; X=1-142. DR PDB; 6FT6; EM; 3.90 A; X=1-142. DR PDB; 6GQ1; EM; 4.40 A; X=22-142. DR PDB; 6GQB; EM; 3.90 A; X=22-142. DR PDB; 6GQV; EM; 4.00 A; X=22-142. DR PDB; 6HD7; EM; 3.40 A; Z=1-142. DR PDB; 6HHQ; X-ray; 3.10 A; 8/CZ=1-142. DR PDB; 6I7O; EM; 5.30 A; AH/XH=23-142. DR PDB; 6M62; EM; 3.20 A; X=1-142. DR PDB; 6N8J; EM; 3.50 A; X=1-142. DR PDB; 6N8K; EM; 3.60 A; X=1-142. DR PDB; 6N8L; EM; 3.60 A; X=1-142. DR PDB; 6N8M; EM; 3.50 A; k=1-142. DR PDB; 6N8N; EM; 3.80 A; k=1-142. DR PDB; 6N8O; EM; 3.50 A; k=1-142. DR PDB; 6OIG; EM; 3.80 A; X=22-142. DR PDB; 6Q8Y; EM; 3.10 A; AH=22-142. DR PDB; 6QIK; EM; 3.10 A; W=1-142. DR PDB; 6QT0; EM; 3.40 A; W=1-142. DR PDB; 6QTZ; EM; 3.50 A; W=1-142. DR PDB; 6R84; EM; 3.60 A; Z=22-142. DR PDB; 6R86; EM; 3.40 A; Z=22-142. DR PDB; 6R87; EM; 3.40 A; Z=22-142. DR PDB; 6RI5; EM; 3.30 A; W=1-142. DR PDB; 6RZZ; EM; 3.20 A; W=1-142. DR PDB; 6S05; EM; 3.90 A; W=1-142. DR PDB; 6S47; EM; 3.28 A; AZ=2-142. DR PDB; 6SNT; EM; 2.80 A; as=1-142. DR PDB; 6SV4; EM; 3.30 A; AH/XH/zH=1-142. DR PDB; 6T4Q; EM; 2.60 A; LX=22-142. DR PDB; 6T7I; EM; 3.20 A; LX=1-142. DR PDB; 6T7T; EM; 3.10 A; LX=22-142. DR PDB; 6T83; EM; 4.00 A; I/Xy=1-142. DR PDB; 6TB3; EM; 2.80 A; AH=22-142. DR PDB; 6TNU; EM; 3.10 A; AH=22-142. DR PDB; 6WOO; EM; 2.90 A; X=22-142. DR PDB; 6XIQ; EM; 4.20 A; X=1-142. DR PDB; 6XIR; EM; 3.20 A; X=1-142. DR PDB; 6YLG; EM; 3.00 A; X=1-142. DR PDB; 6YLH; EM; 3.10 A; X=1-142. DR PDB; 6YLX; EM; 3.90 A; X=1-142. DR PDB; 6YLY; EM; 3.80 A; X=1-142. DR PDB; 6Z6J; EM; 3.40 A; LX=1-142. DR PDB; 6Z6K; EM; 3.40 A; LX=1-142. DR PDB; 7AZY; EM; 2.88 A; I=1-142. DR PDB; 7B7D; EM; 3.30 A; LT=22-142. DR PDB; 7BT6; EM; 3.12 A; X=1-142. DR PDB; 7BTB; EM; 3.22 A; X=1-142. DR PDB; 7MPI; EM; 3.05 A; AX=22-142. DR PDB; 7MPJ; EM; 2.70 A; AX=22-142. DR PDB; 7N8B; EM; 3.05 A; AX=22-142. DR PDB; 7NAC; EM; 3.04 A; X=1-142. DR PDB; 7NAD; EM; 3.04 A; X=1-142. DR PDB; 7NRC; EM; 3.90 A; LZ=22-142. DR PDB; 7NRD; EM; 4.36 A; LZ=22-142. DR PDB; 7OF1; EM; 3.10 A; X=1-142. DR PDB; 7OH3; EM; 3.40 A; X=1-142. DR PDB; 7OHQ; EM; 3.10 A; X=1-142. DR PDB; 7OHR; EM; 4.72 A; X=1-142. DR PDB; 7OHV; EM; 3.90 A; X=1-142. DR PDB; 7R6Q; EM; 2.98 A; X=1-142. DR PDB; 7R72; EM; 3.07 A; X=1-142. DR PDB; 7R7A; EM; 3.04 A; X=1-142. DR PDB; 7TOO; EM; 2.70 A; AL25=1-142. DR PDB; 7TOP; EM; 2.40 A; AL25=1-142. DR PDB; 7U0H; EM; 2.76 A; X=1-142. DR PDB; 7UG6; EM; 2.90 A; X=1-142. DR PDB; 7UOO; EM; 2.34 A; X=1-142. DR PDB; 7UQB; EM; 2.43 A; X=1-142. DR PDB; 7UQZ; EM; 2.44 A; X=1-142. DR PDB; 7V08; EM; 2.36 A; X=1-142. DR PDB; 7Z34; EM; 3.80 A; X=1-142. DR PDB; 7ZPQ; EM; 3.47 A; BW=22-142. DR PDB; 7ZRS; EM; 4.80 A; BW=22-142. DR PDB; 7ZS5; EM; 3.20 A; BY=22-142. DR PDB; 7ZUW; EM; 4.30 A; BW=22-142. DR PDB; 7ZUX; EM; 2.50 A; EW=22-142. DR PDB; 7ZW0; EM; 2.40 A; La=1-142. DR PDB; 8AAF; EM; 2.50 A; K=1-142. DR PDB; 8AGT; EM; 2.60 A; K=1-142. DR PDB; 8AGU; EM; 2.70 A; K=1-142. DR PDB; 8AGV; EM; 2.60 A; K=1-142. DR PDB; 8AGW; EM; 2.60 A; K=1-142. DR PDB; 8AGX; EM; 2.40 A; K=1-142. DR PDB; 8AGZ; EM; 2.60 A; K=1-142. DR PDB; 8BIP; EM; 3.10 A; LX=22-142. DR PDB; 8BJQ; EM; 3.80 A; LX=22-142. DR PDB; 8BN3; EM; 2.40 A; N5=22-142. DR PDB; 8BQD; EM; 3.90 A; AH=22-142. DR PDB; 8BQX; EM; 3.80 A; AH=22-142. DR PDB; 8CCS; EM; 1.97 A; J=1-142. DR PDB; 8CDL; EM; 2.72 A; J=1-142. DR PDB; 8CDR; EM; 2.04 A; J=1-142. DR PDB; 8CEH; EM; 2.05 A; J=1-142. DR PDB; 8CF5; EM; 2.71 A; J=1-142. DR PDB; 8CG8; EM; 2.57 A; J=1-142. DR PDB; 8CGN; EM; 2.28 A; J=1-142. DR PDB; 8CIV; EM; 2.47 A; J=1-142. DR PDB; 8CKU; EM; 3.11 A; J=1-142. DR PDB; 8CMJ; EM; 3.79 A; J=1-142. DR PDB; 8EUB; EM; 2.52 A; AX=1-142. DR PDB; 8EVP; EM; 2.38 A; AX=1-142. DR PDB; 8EVQ; EM; 2.72 A; AX=1-142. DR PDB; 8EVR; EM; 2.87 A; AX=1-142. DR PDB; 8EVS; EM; 2.62 A; AX=1-142. DR PDB; 8EVT; EM; 2.20 A; AX=1-142. DR PDB; 8EWB; EM; 2.87 A; AX=1-142. DR PDB; 8EWC; EM; 2.45 A; AX=1-142. DR PDB; 8HFR; EM; 2.64 A; Xc=1-142. DR PDB; 8K2D; EM; 3.20 A; LX=1-142. DR PDB; 8K82; EM; 3.00 A; LX=1-142. DR PDB; 8P4V; X-ray; 3.16 A; 8/CZ=1-142. DR PDB; 8P85; X-ray; 2.90 A; 8/CZ=1-142. DR PDB; 8P8M; EM; 2.66 A; QX=1-142. DR PDB; 8P8N; EM; 2.15 A; QX=1-142. DR PDB; 8P8U; EM; 2.23 A; QX=1-142. DR PDB; 8P9A; X-ray; 2.90 A; 8/CZ=1-142. DR PDB; 8PFR; EM; 2.15 A; QX=1-142. DR PDB; 8PNN; X-ray; 2.90 A; 8/CZ=1-142. DR PDB; 8T2X; EM; 2.46 A; AX=1-142. DR PDB; 8T2Y; EM; 2.20 A; AX=1-142. DR PDB; 8T2Z; EM; 2.40 A; AX=1-142. DR PDB; 8T30; EM; 2.88 A; AX=1-142. DR PDB; 8T3A; EM; 2.86 A; AX=1-142. DR PDB; 8T3B; EM; 3.08 A; AX=1-142. DR PDB; 8T3C; EM; 3.86 A; AX=1-142. DR PDB; 8T3D; EM; 2.95 A; AX=1-142. DR PDB; 8T3E; EM; 3.04 A; AX=1-142. DR PDB; 8T3F; EM; 3.09 A; AX=1-142. DR PDB; 8UT0; EM; 3.22 A; LZ=22-142. DR PDB; 8UTI; EM; 3.13 A; LZ=22-142. DR PDB; 8V87; EM; 2.66 A; X=1-142. DR PDB; 8XU8; EM; 3.40 A; Z=22-142. DR PDB; 8Y0U; EM; 3.59 A; LX=1-142. DR PDB; 8YLD; EM; 3.90 A; Z=22-142. DR PDB; 8YLR; EM; 3.90 A; Z=22-142. DR PDB; 8Z70; EM; 3.20 A; Z=22-142. DR PDB; 8Z71; EM; 3.60 A; Z=22-142. DR PDB; 8ZGR; EM; 2.70 A; LZ=22-142. DR PDB; 8ZGY; EM; 2.80 A; LZ=22-142. DR PDB; 8ZH3; EM; 2.70 A; LZ=22-142. DR PDB; 8ZHB; EM; 2.60 A; LZ=22-142. DR PDB; 8ZHC; EM; 2.30 A; LZ=22-142. DR PDB; 9F58; EM; 3.10 A; z=1-142. DR PDB; 9F9S; EM; 2.90 A; Lt/Mt=1-142. DR PDB; 9OFV; EM; 3.16 A; b0=1-142. DR PDB; 9R9O; EM; 2.90 A; LX=1-142. DR PDB; 9R9P; EM; 3.00 A; LX=1-142. DR AlphaFoldDB; P04456; -. DR EMDB; EMD-0047; -. DR EMDB; EMD-0048; -. DR EMDB; EMD-0049; -. DR EMDB; EMD-0202; -. DR EMDB; EMD-0369; -. DR EMDB; EMD-0370; -. DR EMDB; EMD-0371; -. DR EMDB; EMD-0372; -. DR EMDB; EMD-0373; -. DR EMDB; EMD-0374; -. DR EMDB; EMD-10068; -. DR EMDB; EMD-10071; -. DR EMDB; EMD-10098; -. DR EMDB; EMD-10262; -. DR EMDB; EMD-10315; -. DR EMDB; EMD-10377; -. DR EMDB; EMD-10396; -. DR EMDB; EMD-10397; -. DR EMDB; EMD-10398; -. DR EMDB; EMD-10431; -. DR EMDB; EMD-10537; -. DR EMDB; EMD-10838; -. DR EMDB; EMD-10839; -. DR EMDB; EMD-10841; -. DR EMDB; EMD-10842; -. DR EMDB; EMD-11096; -. DR EMDB; EMD-11097; -. DR EMDB; EMD-11951; -. DR EMDB; EMD-12081; -. DR EMDB; EMD-12534; -. DR EMDB; EMD-12535; -. DR EMDB; EMD-12866; -. DR EMDB; EMD-12892; -. DR EMDB; EMD-12905; -. DR EMDB; EMD-12906; -. DR EMDB; EMD-12910; -. DR EMDB; EMD-14471; -. DR EMDB; EMD-14861; -. DR EMDB; EMD-14921; -. DR EMDB; EMD-14926; -. DR EMDB; EMD-14978; -. DR EMDB; EMD-14979; -. DR EMDB; EMD-14990; -. DR EMDB; EMD-15296; -. DR EMDB; EMD-15423; -. DR EMDB; EMD-15424; -. DR EMDB; EMD-15425; -. DR EMDB; EMD-15426; -. DR EMDB; EMD-15427; -. DR EMDB; EMD-15428; -. DR EMDB; EMD-16086; -. DR EMDB; EMD-16090; -. DR EMDB; EMD-16127; -. DR EMDB; EMD-16182; -. DR EMDB; EMD-16191; -. DR EMDB; EMD-16563; -. DR EMDB; EMD-16591; -. DR EMDB; EMD-16594; -. DR EMDB; EMD-16609; -. DR EMDB; EMD-16616; -. DR EMDB; EMD-16634; -. DR EMDB; EMD-16648; -. DR EMDB; EMD-16684; -. DR EMDB; EMD-16702; -. DR EMDB; EMD-16729; -. DR EMDB; EMD-17549; -. DR EMDB; EMD-17550; -. DR EMDB; EMD-17552; -. DR EMDB; EMD-17653; -. DR EMDB; EMD-20077; -. DR EMDB; EMD-21859; -. DR EMDB; EMD-22196; -. DR EMDB; EMD-22198; -. DR EMDB; EMD-23934; -. DR EMDB; EMD-23935; -. DR EMDB; EMD-24235; -. DR EMDB; EMD-24269; -. DR EMDB; EMD-24270; -. DR EMDB; EMD-24286; -. DR EMDB; EMD-24290; -. DR EMDB; EMD-24296; -. DR EMDB; EMD-26033; -. DR EMDB; EMD-26034; -. DR EMDB; EMD-26259; -. DR EMDB; EMD-26485; -. DR EMDB; EMD-26651; -. DR EMDB; EMD-26686; -. DR EMDB; EMD-26703; -. DR EMDB; EMD-26941; -. DR EMDB; EMD-28610; -. DR EMDB; EMD-28632; -. DR EMDB; EMD-28633; -. DR EMDB; EMD-28634; -. DR EMDB; EMD-28635; -. DR EMDB; EMD-28636; -. DR EMDB; EMD-28642; -. DR EMDB; EMD-28643; -. DR EMDB; EMD-30108; -. DR EMDB; EMD-30170; -. DR EMDB; EMD-30174; -. DR EMDB; EMD-3461; -. DR EMDB; EMD-34725; -. DR EMDB; EMD-36839; -. DR EMDB; EMD-36945; -. DR EMDB; EMD-38660; -. DR EMDB; EMD-40990; -. DR EMDB; EMD-40991; -. DR EMDB; EMD-40992; -. DR EMDB; EMD-40993; -. DR EMDB; EMD-40997; -. DR EMDB; EMD-40998; -. DR EMDB; EMD-40999; -. DR EMDB; EMD-41000; -. DR EMDB; EMD-41001; -. DR EMDB; EMD-41002; -. DR EMDB; EMD-4140; -. DR EMDB; EMD-42525; -. DR EMDB; EMD-42540; -. DR EMDB; EMD-4302; -. DR EMDB; EMD-43027; -. DR EMDB; EMD-4427; -. DR EMDB; EMD-4474; -. DR EMDB; EMD-4560; -. DR EMDB; EMD-4630; -. DR EMDB; EMD-4636; -. DR EMDB; EMD-4751; -. DR EMDB; EMD-4752; -. DR EMDB; EMD-4753; -. DR EMDB; EMD-4884; -. DR EMDB; EMD-50188; -. DR EMDB; EMD-50259; -. DR EMDB; EMD-53860; -. DR EMDB; EMD-53861; -. DR EMDB; EMD-60088; -. DR EMDB; EMD-60091; -. DR EMDB; EMD-60094; -. DR EMDB; EMD-60097; -. DR EMDB; EMD-60098; -. DR EMDB; EMD-70444; -. DR EMDB; EMD-8362; -. DR EMDB; EMD-8368; -. DR SMR; P04456; -. DR BioGRID; 34248; 644. DR DIP; DIP-7137N; -. DR FunCoup; P04456; 1032. DR IntAct; P04456; 143. DR MINT; P04456; -. DR STRING; 4932.YOL127W; -. DR iPTMnet; P04456; -. DR PaxDb; 4932-YOL127W; -. DR PeptideAtlas; P04456; -. DR TopDownProteomics; P04456; -. DR EnsemblFungi; YOL127W_mRNA; YOL127W; YOL127W. DR GeneID; 853993; -. DR KEGG; sce:YOL127W; -. DR AGR; SGD:S000005487; -. DR SGD; S000005487; RPL25. DR VEuPathDB; FungiDB:YOL127W; -. DR eggNOG; KOG1751; Eukaryota. DR HOGENOM; CLU_037562_0_1_1; -. DR InParanoid; P04456; -. DR OMA; RLDHHKV; -. DR OrthoDB; 1267328at2759; -. DR BioCyc; YEAST:G3O-33522-MONOMER; -. 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 Reactome; R-SCE-9954709; Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide. DR Reactome; R-SCE-9954714; PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA. DR BioGRID-ORCS; 853993; 2 hits in 10 CRISPR screens. DR EvolutionaryTrace; P04456; -. DR PRO; PR:P04456; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; P04456; protein. DR GO; GO:0005737; C:cytoplasm; EXP:UniProtKB. 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:0003723; F:RNA binding; IDA:SGD. DR GO; GO:0019843; F:rRNA binding; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IC:SGD. DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD. DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD. DR FunFam; 3.30.70.330:FF:000035; 60S ribosomal protein L23a; 1. DR Gene3D; 3.30.70.330; -; 1. DR HAMAP; MF_01369_A; Ribosomal_uL23_A; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR013025; Ribosomal_uL23-like. DR InterPro; IPR012678; Ribosomal_uL23/eL15/eS24_sf. DR InterPro; IPR001014; Ribosomal_uL23_CS. DR InterPro; IPR005633; Ribosomal_uL23_N. DR NCBIfam; NF011118; PRK14548.1; 1. DR PANTHER; PTHR11620; 60S RIBOSOMAL PROTEIN L23A; 1. DR Pfam; PF00276; Ribosomal_L23; 1. DR Pfam; PF03939; Ribosomal_L23eN; 1. DR SUPFAM; SSF54189; Ribosomal proteins S24e, L23 and L15e; 1. DR PROSITE; PS00050; RIBOSOMAL_L23; 1. 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; 4V5Z; -. 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; 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; 6CB1; -. 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; 7MPI; -. DR PDBsum; 7MPJ; -. DR PDBsum; 7N8B; -. DR PDBsum; 7NAC; -. DR PDBsum; 7NAD; -. DR PDBsum; 7NRC; -. DR PDBsum; 7NRD; -. DR PDBsum; 7OF1; -. DR PDBsum; 7OH3; -. DR PDBsum; 7OHQ; -. DR PDBsum; 7OHR; -. DR PDBsum; 7OHV; -. DR PDBsum; 7R6Q; -. DR PDBsum; 7R72; -. DR PDBsum; 7R7A; -. DR PDBsum; 7TOO; -. DR PDBsum; 7TOP; -. DR PDBsum; 7U0H; -. DR PDBsum; 7UG6; -. DR PDBsum; 7UOO; -. DR PDBsum; 7UQB; -. DR PDBsum; 7UQZ; -. DR PDBsum; 7V08; -. DR PDBsum; 7Z34; -. DR PDBsum; 7ZPQ; -. DR PDBsum; 7ZRS; -. DR PDBsum; 7ZS5; -. DR PDBsum; 7ZUW; -. DR PDBsum; 7ZUX; -. DR PDBsum; 7ZW0; -. DR PDBsum; 8AAF; -. DR PDBsum; 8AGT; -. DR PDBsum; 8AGU; -. DR PDBsum; 8AGV; -. DR PDBsum; 8AGW; -. DR PDBsum; 8AGX; -. DR PDBsum; 8AGZ; -. DR PDBsum; 8BIP; -. DR PDBsum; 8BJQ; -. DR PDBsum; 8BN3; -. DR PDBsum; 8BQD; -. DR PDBsum; 8BQX; -. DR PDBsum; 8CCS; -. DR PDBsum; 8CDL; -. DR PDBsum; 8CDR; -. DR PDBsum; 8CEH; -. DR PDBsum; 8CF5; -. DR PDBsum; 8CG8; -. DR PDBsum; 8CGN; -. DR PDBsum; 8CIV; -. DR PDBsum; 8CKU; -. DR PDBsum; 8CMJ; -. DR PDBsum; 8EUB; -. DR PDBsum; 8EVP; -. DR PDBsum; 8EVQ; -. DR PDBsum; 8EVR; -. DR PDBsum; 8EVS; -. DR PDBsum; 8EVT; -. DR PDBsum; 8EWB; -. DR PDBsum; 8EWC; -. DR PDBsum; 8HFR; -. DR PDBsum; 8K2D; -. DR PDBsum; 8K82; -. DR PDBsum; 8P4V; -. DR PDBsum; 8P85; -. DR PDBsum; 8P8M; -. DR PDBsum; 8P8N; -. DR PDBsum; 8P8U; -. DR PDBsum; 8P9A; -. DR PDBsum; 8PFR; -. DR PDBsum; 8PNN; -. DR PDBsum; 8T2X; -. DR PDBsum; 8T2Y; -. DR PDBsum; 8T2Z; -. DR PDBsum; 8T30; -. DR PDBsum; 8T3A; -. DR PDBsum; 8T3B; -. DR PDBsum; 8T3C; -. DR PDBsum; 8T3D; -. DR PDBsum; 8T3E; -. DR PDBsum; 8T3F; -. DR PDBsum; 8UT0; -. DR PDBsum; 8UTI; -. DR PDBsum; 8V87; -. DR PDBsum; 8XU8; -. DR PDBsum; 8Y0U; -. DR PDBsum; 8YLD; -. DR PDBsum; 8YLR; -. DR PDBsum; 8Z70; -. DR PDBsum; 8Z71; -. DR PDBsum; 8ZGR; -. DR PDBsum; 8ZGY; -. DR PDBsum; 8ZH3; -. DR PDBsum; 8ZHB; -. DR PDBsum; 8ZHC; -. DR PDBsum; 9F58; -. DR PDBsum; 9F9S; -. DR PDBsum; 9OFV; -. DR PDBsum; 9R9O; -. DR PDBsum; 9R9P; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:10601260, FT ECO:0000269|PubMed:1544921" FT CHAIN 2..142 FT /note="Large ribosomal subunit protein uL23" FT /id="PRO_0000129483" FT CROSSLNK 61 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:15542864" FT CONFLICT 106..112 FT /note="DVLKVNT -> NI (in Ref. 1; CAA25506)" FT /evidence="ECO:0000305" FT HELIX 5..16 FT /evidence="ECO:0007829|PDB:7UOO" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:6M62" FT HELIX 24..26 FT /evidence="ECO:0007829|PDB:8T2Y" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 48..51 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 52..55 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 59..62 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 63..66 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 70..79 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 81..86 FT /evidence="ECO:0007829|PDB:8CCS" FT HELIX 92..103 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 107..114 FT /evidence="ECO:0007829|PDB:8CCS" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:7ZUX" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:8CCS" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:6TB3" FT HELIX 132..139 FT /evidence="ECO:0007829|PDB:8CCS" SQ SEQUENCE 142 AA; 15758 MW; E40ED3A4FB8CA9F5 CRC64; MAPSAKATAA KKAVVKGTNG KKALKVRTSA TFRLPKTLKL ARAPKYASKA VPHYNRLDSY KVIEQPITSE TAMKKVEDGN ILVFQVSMKA NKYQIKKAVK ELYEVDVLKV NTLVRPNGTK KAYVRLTADY DALDIANRIG YI //