ID RL11B_YEAST Reviewed; 174 AA. AC Q3E757; D6VUL7; P06380; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 22-FEB-2023, entry version 151. DE RecName: Full=60S ribosomal protein L11-B {ECO:0000303|PubMed:9559554}; DE AltName: Full=L16; DE AltName: Full=Large ribosomal subunit protein uL5-B {ECO:0000303|PubMed:24524803}; DE AltName: Full=RP39; DE AltName: Full=YL22; GN Name=RPL11B {ECO:0000303|PubMed:9559554}; Synonyms=RP39B, RPL16B; GN OrderedLocusNames=YGR085C; 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=6390341; DOI=10.1093/nar/12.22.8295; RA Teem J.L., Abovich N., Kaufer N.F., Schwindinger W.F., Warner J.R., RA Levy A., Woolford J.L. Jr., Leer R.J., van Raamsdonk-Duin M.M.C., RA Mager W.H., Planta R.J., Schultz L., Friesen J.D., Fried H.M., Rosbash M.; RT "A comparison of yeast ribosomal protein gene DNA sequences."; RL Nucleic Acids Res. 12:8295-8312(1984). RN [2] 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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. RX PubMed=3023862; DOI=10.1128/mcb.6.2.674-687.1986; RA Rotenberg M.O., Woolford J.L. Jr.; RT "Tripartite upstream promoter element essential for expression of RT Saccharomyces cerevisiae ribosomal protein genes."; RL Mol. Cell. Biol. 6:674-687(1986). RN [5] 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 [6] RP CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-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 [7] 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 [8] 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 [9] RP SUBUNIT, AND 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). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 METHYLATION AT LYS-75. RX PubMed=22522802; DOI=10.1002/pmic.201100570; RA Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.; RT "Methylation of translation-associated proteins in Saccharomyces RT cerevisiae: Identification of methylated lysines and their RT methyltransferases."; RL Proteomics 12:960-972(2012). RN [12] RP INTERACTION WITH RPL5 AND SYO1, AND SUBCELLULAR LOCATION. RX PubMed=23118189; DOI=10.1126/science.1226960; RA Kressler D., Bange G., Ogawa Y., Stjepanovic G., Bradatsch B., Pratte D., RA Amlacher S., Strauss D., Yoneda Y., Katahira J., Sinning I., Hurt E.; RT "Synchronizing nuclear import of ribosomal proteins with ribosome RT assembly."; RL Science 338:666-671(2012). RN [13] 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 [14] RP STRUCTURE BY ELECTRON MICROSCOPY (7.3 ANGSTROMS) OF 7-171. RX PubMed=17115051; DOI=10.1038/nsmb1177; RA Schueler M., Connell S.R., Lescoute A., Giesebrecht J., Dabrowski M., RA Schroeer B., Mielke T., Penczek P.A., Westhof E., Spahn C.M.T.; RT "Structure of the ribosome-bound cricket paralysis virus IRES RNA."; RL Nat. Struct. Mol. Biol. 13:1092-1096(2006). 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). uL5 CC forms a heterotrimeric complex with uL18/RPL5 and SYO1. Interaction of CC this complex with KAP104 allows the nuclear import of the heterotrimer CC (PubMed:23118189). {ECO:0000269|PubMed:22096102, CC ECO:0000269|PubMed:23118189, ECO:0000305|PubMed:9559554}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus CC {ECO:0000269|PubMed:23118189}. Note=The SYO1-uL5-uL18 complex is CC transported into the nucleus by KAP104. {ECO:0000269|PubMed:23118189}. CC -!- PTM: N-terminally acetylated by acetyltransferase NatA. CC {ECO:0000269|PubMed:10601260}. CC -!- MISCELLANEOUS: Present with 21200 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- MISCELLANEOUS: There are 2 genes for uL5 in yeast. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 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; Z72870; CAA97087.1; -; Genomic_DNA. DR EMBL; M12933; AAA34990.1; -; Genomic_DNA. DR EMBL; BK006941; DAA08178.1; -; Genomic_DNA. DR PIR; A02764; R5BY16. DR RefSeq; NP_011599.1; NM_001181214.1. DR PDB; 2NOQ; EM; 7.30 A; H=7-171. DR PDB; 3J0Q; EM; 10.60 A; k=7-171. DR PDB; 4U3M; X-ray; 3.00 A; M1/m1=2-174. DR PDB; 4U3N; X-ray; 3.20 A; M1/m1=2-174. DR PDB; 4U3U; X-ray; 2.90 A; M1/m1=2-174. DR PDB; 4U4N; X-ray; 3.10 A; M1/m1=2-174. DR PDB; 4U4O; X-ray; 3.60 A; M1/m1=2-174. DR PDB; 4U4Q; X-ray; 3.00 A; M1/m1=2-174. DR PDB; 4U4R; X-ray; 2.80 A; M1/m1=2-174. DR PDB; 4U4U; X-ray; 3.00 A; M1/m1=2-174. DR PDB; 4U4Y; X-ray; 3.20 A; M1/m1=2-174. DR PDB; 4U4Z; X-ray; 3.10 A; M1/m1=2-174. DR PDB; 4U50; X-ray; 3.20 A; M1/m1=2-174. DR PDB; 4U51; X-ray; 3.20 A; M1/m1=2-174. DR PDB; 4U52; X-ray; 3.00 A; M1/m1=2-174. DR PDB; 4U53; X-ray; 3.30 A; M1/m1=2-174. DR PDB; 4U55; X-ray; 3.20 A; M1/m1=2-174. DR PDB; 4U56; X-ray; 3.45 A; M1/m1=2-174. DR PDB; 4U6F; X-ray; 3.10 A; M1/m1=2-174. DR PDB; 4V8T; EM; 8.10 A; J=1-174. DR PDB; 5DAT; X-ray; 3.15 A; M1/m1=2-174. DR PDB; 5DC3; X-ray; 3.25 A; M1/m1=2-174. DR PDB; 5DGF; X-ray; 3.30 A; M1/m1=2-174. DR PDB; 5DGV; X-ray; 3.10 A; M1/m1=2-174. DR PDB; 5I4L; X-ray; 3.10 A; M1/m1=6-174. DR PDB; 5LYB; X-ray; 3.25 A; M1/m1=6-174. DR PDB; 5MEI; X-ray; 3.50 A; CM/s=6-174. DR PDB; 5NDV; X-ray; 3.30 A; M1/m1=6-174. DR PDB; 5NDW; X-ray; 3.70 A; M1/m1=6-174. DR PDB; 5OBM; X-ray; 3.40 A; M1/m1=6-174. DR PDB; 5ON6; X-ray; 3.10 A; CM/s=6-174. DR PDB; 5TBW; X-ray; 3.00 A; CM/s=6-174. DR PDB; 5TGA; X-ray; 3.30 A; M1/m1=6-174. DR PDB; 5TGM; X-ray; 3.50 A; M1/m1=6-174. DR PDB; 6GQ1; EM; 4.40 A; J=6-174. DR PDB; 6GQB; EM; 3.90 A; J=6-174. DR PDB; 6GQV; EM; 4.00 A; J=6-174. DR PDB; 6HHQ; X-ray; 3.10 A; CM/s=1-174. DR PDB; 6I7O; EM; 5.30 A; AG/XG=6-174. DR PDB; 6OIG; EM; 3.80 A; J=6-174. DR PDB; 6Q8Y; EM; 3.10 A; AG=6-174. DR PDB; 6R84; EM; 3.60 A; M=6-174. DR PDB; 6R86; EM; 3.40 A; M=6-174. DR PDB; 6R87; EM; 3.40 A; M=6-174. DR PDB; 6S47; EM; 3.28 A; AM=6-174. DR PDB; 6T4Q; EM; 2.60 A; LJ=6-174. DR PDB; 6TB3; EM; 2.80 A; AG=6-174. DR PDB; 6TNU; EM; 3.10 A; AG=6-174. DR PDB; 6WOO; EM; 2.90 A; J=6-173. DR PDB; 7AZY; EM; 2.88 A; h=1-174. DR PDB; 7B7D; EM; 3.30 A; LM=6-174. DR PDB; 7NRC; EM; 3.90 A; LM=6-174. DR PDB; 7NRD; EM; 4.36 A; LM=6-174. DR PDBsum; 2NOQ; -. DR PDBsum; 3J0Q; -. 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; 4V8T; -. DR PDBsum; 5DAT; -. DR PDBsum; 5DC3; -. DR PDBsum; 5DGF; -. DR PDBsum; 5DGV; -. DR PDBsum; 5I4L; -. DR PDBsum; 5LYB; -. DR PDBsum; 5MEI; -. DR PDBsum; 5NDV; -. DR PDBsum; 5NDW; -. DR PDBsum; 5OBM; -. DR PDBsum; 5ON6; -. DR PDBsum; 5TBW; -. DR PDBsum; 5TGA; -. DR PDBsum; 5TGM; -. DR PDBsum; 6GQ1; -. DR PDBsum; 6GQB; -. DR PDBsum; 6GQV; -. DR PDBsum; 6HHQ; -. DR PDBsum; 6I7O; -. DR PDBsum; 6OIG; -. DR PDBsum; 6Q8Y; -. DR PDBsum; 6R84; -. DR PDBsum; 6R86; -. DR PDBsum; 6R87; -. DR PDBsum; 6S47; -. DR PDBsum; 6T4Q; -. DR PDBsum; 6TB3; -. DR PDBsum; 6TNU; -. DR PDBsum; 6WOO; -. DR PDBsum; 7AZY; -. DR PDBsum; 7B7D; -. DR PDBsum; 7NRC; -. DR PDBsum; 7NRD; -. DR AlphaFoldDB; Q3E757; -. DR SMR; Q3E757; -. DR BioGRID; 33327; 313. DR DIP; DIP-29386N; -. DR IntAct; Q3E757; 24. DR MINT; Q3E757; -. DR STRING; 4932.YGR085C; -. DR iPTMnet; Q3E757; -. DR MaxQB; Q3E757; -. DR PaxDb; Q3E757; -. DR PeptideAtlas; Q3E757; -. DR EnsemblFungi; YGR085C_mRNA; YGR085C; YGR085C. DR GeneID; 852976; -. DR KEGG; sce:YGR085C; -. DR AGR; SGD:S000003317; -. DR SGD; S000003317; RPL11B. DR VEuPathDB; FungiDB:YGR085C; -. DR eggNOG; KOG0397; Eukaryota. DR GeneTree; ENSGT00910000144211; -. DR HOGENOM; CLU_061015_3_0_1; -. DR InParanoid; Q3E757; -. DR OMA; MDFYCIM; -. DR OrthoDB; 5473480at2759; -. DR BioCyc; YEAST:G3O-30797-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 BioGRID-ORCS; 852976; 3 hits in 10 CRISPR screens. DR EvolutionaryTrace; Q3E757; -. DR PRO; PR:Q3E757; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; Q3E757; protein. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD. DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD. DR Gene3D; 3.30.1440.10; -; 1. DR InterPro; IPR002132; Ribosomal_L5. DR InterPro; IPR031309; Ribosomal_L5_C. DR InterPro; IPR020929; Ribosomal_L5_CS. DR InterPro; IPR022803; Ribosomal_L5_dom_sf. DR InterPro; IPR031310; Ribosomal_L5_N. DR PANTHER; PTHR11994:SF8; 60S RIBOSOMAL PROTEIN L11; 1. DR PANTHER; PTHR11994; 60S RIBOSOMAL PROTEIN L11-RELATED; 1. DR Pfam; PF00281; Ribosomal_L5; 1. DR Pfam; PF00673; Ribosomal_L5_C; 1. DR PIRSF; PIRSF002161; Ribosomal_L5; 1. DR SUPFAM; SSF55282; RL5-like; 1. DR PROSITE; PS00358; RIBOSOMAL_L5; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Methylation; Nucleus; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:10601260, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..174 FT /note="60S ribosomal protein L11-B" FT /id="PRO_0000125105" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:10601260, FT ECO:0007744|PubMed:22814378" FT MOD_RES 75 FT /note="N6,N6,N6-trimethyllysine" FT /evidence="ECO:0000269|PubMed:22522802" FT CONFLICT 138 FT /note="V -> A (in Ref. 1)" FT /evidence="ECO:0000305" FT STRAND 14..21 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:4U4U" FT HELIX 28..41 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 74..86 FT /evidence="ECO:0007829|PDB:4U4R" FT TURN 87..89 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 93..96 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:4U4R" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 125..131 FT /evidence="ECO:0007829|PDB:4U4R" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 137..140 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 141..144 FT /evidence="ECO:0007829|PDB:4U4Q" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:4U4R" FT HELIX 156..164 FT /evidence="ECO:0007829|PDB:4U4R" FT TURN 165..167 FT /evidence="ECO:0007829|PDB:4U4R" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:4U4R" SQ SEQUENCE 174 AA; 19750 MW; 04F6CD88FEBD63E4 CRC64; MSTKAQNPMR DLKIEKLVLN ISVGESGDRL TRASKVLEQL SGQTPVQSKA RYTVRTFGIR RNEKIAVHVT VRGPKAEEIL ERGLKVKEYQ LRDRNFSATG NFGFGIDEHI DLGIKYDPSI GIFGMDFYVV MNRPGARVTR RKRCKGTVGN SHKTTKEDTV SWFKQKYDAD VLDK //