RL11B_YEAST
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 03-AUG-2022, entry version 148.
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}.
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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; 310.
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 PRIDE; Q3E757; -.
DR EnsemblFungi; YGR085C_mRNA; YGR085C; YGR085C.
DR GeneID; 852976; -.
DR KEGG; sce:YGR085C; -.
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 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 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; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 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
