ID RM49_HUMAN Reviewed; 166 AA. AC Q13405; B2R4G6; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 180. DE RecName: Full=Large ribosomal subunit protein mL49 {ECO:0000303|PubMed:25278503}; DE AltName: Full=39S ribosomal protein L49, mitochondrial; DE Short=L49mt; DE Short=MRP-L49; DE AltName: Full=Neighbor of FAU; DE Short=NOF; DE AltName: Full=Protein NOF1; GN Name=MRPL49; Synonyms=C11orf4, NOF1; ORFNames=OK/SW-cl.67; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=8786148; DOI=10.1006/geno.1996.0310; RA Kas K., Lemahieu V., Meyen E., van de Ven W.J.M., Merregaert J.; RT "Isolation, cDNA, and genomic structure of a conserved gene (NOF) at RT chromosome 11q13 next to FAU and oriented in the opposite transcriptional RT orientation."; RL Genomics 34:433-436(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP IDENTIFICATION, AND SUBUNIT. RX PubMed=11551941; DOI=10.1074/jbc.m106510200; RA Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M., RA Moseley A., Spremulli L.L.; RT "The large subunit of the mammalian mitochondrial ribosome. Analysis of the RT complement of ribosomal proteins present."; RL J. Biol. Chem. 276:43958-43969(2001). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [9] {ECO:0007744|PDB:3J7Y} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=25278503; DOI=10.1126/science.1258026; RA Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G., RA Scheres S.H., Ramakrishnan V.; RT "Structure of the large ribosomal subunit from human mitochondria."; RL Science 346:718-722(2014). RN [10] {ECO:0007744|PDB:3J9M} RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=25838379; DOI=10.1126/science.aaa1193; RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.; RT "Ribosome. The structure of the human mitochondrial ribosome."; RL Science 348:95-98(2015). RN [11] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM} RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=28892042; DOI=10.1038/nsmb.3464; RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J., RA Amunts A., Ramakrishnan V.; RT "Structures of the human mitochondrial ribosome in native states of RT assembly."; RL Nat. Struct. Mol. Biol. 24:866-869(2017). CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt- CC LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503). Mature CC mammalian 55S mitochondrial ribosomes consist of a small (28S) and a CC large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA CC (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains CC a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA CC (mt-tRNA(Val)), which plays an integral structural role, and 52 CC different proteins (PubMed:11551941, PubMed:25278503, PubMed:25838379). CC Interacts with OXA1L (By similarity). {ECO:0000250|UniProtKB:Q5EA71, CC ECO:0000269|PubMed:11551941, ECO:0000269|PubMed:25278503, CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}. CC -!- INTERACTION: CC Q13405; Q86V38: ATN1; NbExp=3; IntAct=EBI-5325200, EBI-11954292; CC Q13405; P23560-2: BDNF; NbExp=3; IntAct=EBI-5325200, EBI-12275524; CC Q13405; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-5325200, EBI-1055254; CC Q13405; P16284: PECAM1; NbExp=3; IntAct=EBI-5325200, EBI-716404; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503, CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein CC mL49 family. {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; U39400; AAB18826.1; -; mRNA. DR EMBL; AB062395; BAB93482.1; -; mRNA. DR EMBL; AK311821; BAG34763.1; -; mRNA. DR EMBL; CH471076; EAW74355.1; -; Genomic_DNA. DR EMBL; BC004378; AAH04378.1; -; mRNA. DR CCDS; CCDS8096.1; -. DR PIR; G02237; G02237. DR RefSeq; NP_004918.1; NM_004927.3. DR PDB; 3J7Y; EM; 3.40 A; g=1-166. DR PDB; 3J9M; EM; 3.50 A; g=1-166. DR PDB; 5OOL; EM; 3.06 A; g=1-166. DR PDB; 5OOM; EM; 3.03 A; g=1-166. DR PDB; 6I9R; EM; 3.90 A; g=1-166. DR PDB; 6NU2; EM; 3.90 A; g=38-166. DR PDB; 6NU3; EM; 4.40 A; g=1-166. DR PDB; 6VLZ; EM; 2.97 A; g=1-166. DR PDB; 6VMI; EM; 2.96 A; g=1-166. DR PDB; 6ZM5; EM; 2.89 A; g=1-166. DR PDB; 6ZM6; EM; 2.59 A; g=1-166. DR PDB; 6ZS9; EM; 4.00 A; g=1-166. DR PDB; 6ZSA; EM; 4.00 A; g=1-166. DR PDB; 6ZSB; EM; 4.50 A; g=1-166. DR PDB; 6ZSC; EM; 3.50 A; g=1-166. DR PDB; 6ZSD; EM; 3.70 A; g=1-166. DR PDB; 6ZSE; EM; 5.00 A; g=1-166. DR PDB; 6ZSG; EM; 4.00 A; g=1-166. DR PDB; 7A5F; EM; 4.40 A; g3=1-166. DR PDB; 7A5G; EM; 4.33 A; g3=1-166. DR PDB; 7A5H; EM; 3.30 A; g=1-166. DR PDB; 7A5I; EM; 3.70 A; g3=1-166. DR PDB; 7A5J; EM; 3.10 A; g=1-166. DR PDB; 7A5K; EM; 3.70 A; g3=1-166. DR PDB; 7L08; EM; 3.49 A; g=1-166. DR PDB; 7L20; EM; 3.15 A; g=1-166. DR PDB; 7O9K; EM; 3.10 A; g=1-166. DR PDB; 7O9M; EM; 2.50 A; g=1-166. DR PDB; 7ODR; EM; 2.90 A; g=1-166. DR PDB; 7ODS; EM; 3.10 A; g=1-166. DR PDB; 7ODT; EM; 3.10 A; g=1-166. DR PDB; 7OF0; EM; 2.20 A; g=1-166. DR PDB; 7OF2; EM; 2.70 A; g=1-166. DR PDB; 7OF3; EM; 2.70 A; g=1-166. DR PDB; 7OF4; EM; 2.70 A; g=1-166. DR PDB; 7OF5; EM; 2.90 A; g=1-166. DR PDB; 7OF6; EM; 2.60 A; g=1-166. DR PDB; 7OF7; EM; 2.50 A; g=1-166. DR PDB; 7OG4; EM; 3.80 A; g=1-166. DR PDB; 7OI6; EM; 5.70 A; g=1-166. DR PDB; 7OI7; EM; 3.50 A; g=1-166. DR PDB; 7OI8; EM; 3.50 A; g=1-166. DR PDB; 7OI9; EM; 3.30 A; g=1-166. DR PDB; 7OIA; EM; 3.20 A; g=1-166. DR PDB; 7OIB; EM; 3.30 A; g=1-166. DR PDB; 7OIC; EM; 3.10 A; g=1-166. DR PDB; 7OID; EM; 3.70 A; g=1-166. DR PDB; 7OIE; EM; 3.50 A; g=1-166. DR PDB; 7PD3; EM; 3.40 A; g=1-166. DR PDB; 7PO4; EM; 2.56 A; g=1-166. DR PDB; 7QH6; EM; 3.08 A; g=1-166. DR PDB; 7QH7; EM; 2.89 A; g=38-166. DR PDB; 7QI4; EM; 2.21 A; g=1-166. DR PDB; 7QI5; EM; 2.63 A; g=1-166. DR PDB; 7QI6; EM; 2.98 A; g=1-166. DR PDB; 8ANY; EM; 2.85 A; g=1-166. DR PDB; 8OIR; EM; 3.10 A; Bx=1-166. DR PDB; 8OIT; EM; 2.90 A; Bx=1-166. DR PDBsum; 3J7Y; -. DR PDBsum; 3J9M; -. DR PDBsum; 5OOL; -. DR PDBsum; 5OOM; -. DR PDBsum; 6I9R; -. DR PDBsum; 6NU2; -. DR PDBsum; 6NU3; -. DR PDBsum; 6VLZ; -. DR PDBsum; 6VMI; -. DR PDBsum; 6ZM5; -. DR PDBsum; 6ZM6; -. DR PDBsum; 6ZS9; -. DR PDBsum; 6ZSA; -. DR PDBsum; 6ZSB; -. DR PDBsum; 6ZSC; -. DR PDBsum; 6ZSD; -. DR PDBsum; 6ZSE; -. DR PDBsum; 6ZSG; -. DR PDBsum; 7A5F; -. DR PDBsum; 7A5G; -. DR PDBsum; 7A5H; -. DR PDBsum; 7A5I; -. DR PDBsum; 7A5J; -. DR PDBsum; 7A5K; -. DR PDBsum; 7L08; -. DR PDBsum; 7L20; -. DR PDBsum; 7O9K; -. DR PDBsum; 7O9M; -. DR PDBsum; 7ODR; -. DR PDBsum; 7ODS; -. DR PDBsum; 7ODT; -. DR PDBsum; 7OF0; -. DR PDBsum; 7OF2; -. DR PDBsum; 7OF3; -. DR PDBsum; 7OF4; -. DR PDBsum; 7OF5; -. DR PDBsum; 7OF6; -. DR PDBsum; 7OF7; -. DR PDBsum; 7OG4; -. DR PDBsum; 7OI6; -. DR PDBsum; 7OI7; -. DR PDBsum; 7OI8; -. DR PDBsum; 7OI9; -. DR PDBsum; 7OIA; -. DR PDBsum; 7OIB; -. DR PDBsum; 7OIC; -. DR PDBsum; 7OID; -. DR PDBsum; 7OIE; -. DR PDBsum; 7PD3; -. DR PDBsum; 7PO4; -. DR PDBsum; 7QH6; -. DR PDBsum; 7QH7; -. DR PDBsum; 7QI4; -. DR PDBsum; 7QI5; -. DR PDBsum; 7QI6; -. DR PDBsum; 8ANY; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIT; -. DR AlphaFoldDB; Q13405; -. DR EMDB; EMD-0514; -. DR EMDB; EMD-0515; -. DR EMDB; EMD-11278; -. DR EMDB; EMD-11279; -. DR EMDB; EMD-11390; -. DR EMDB; EMD-11391; -. DR EMDB; EMD-11392; -. DR EMDB; EMD-11393; -. DR EMDB; EMD-11394; -. DR EMDB; EMD-11395; -. DR EMDB; EMD-11397; -. DR EMDB; EMD-11641; -. DR EMDB; EMD-11642; -. DR EMDB; EMD-11643; -. DR EMDB; EMD-11644; -. DR EMDB; EMD-11645; -. DR EMDB; EMD-11646; -. DR EMDB; EMD-12763; -. DR EMDB; EMD-12764; -. DR EMDB; EMD-12845; -. DR EMDB; EMD-12846; -. DR EMDB; EMD-12847; -. DR EMDB; EMD-12865; -. DR EMDB; EMD-12867; -. DR EMDB; EMD-12868; -. DR EMDB; EMD-12869; -. DR EMDB; EMD-12870; -. DR EMDB; EMD-12871; -. DR EMDB; EMD-12872; -. DR EMDB; EMD-12877; -. DR EMDB; EMD-12919; -. DR EMDB; EMD-12920; -. DR EMDB; EMD-12921; -. DR EMDB; EMD-12922; -. DR EMDB; EMD-12923; -. DR EMDB; EMD-12924; -. DR EMDB; EMD-12925; -. DR EMDB; EMD-12926; -. DR EMDB; EMD-12927; -. DR EMDB; EMD-13329; -. DR EMDB; EMD-13562; -. DR EMDB; EMD-13965; -. DR EMDB; EMD-13967; -. DR EMDB; EMD-13980; -. DR EMDB; EMD-13981; -. DR EMDB; EMD-13982; -. DR EMDB; EMD-15544; -. DR EMDB; EMD-16897; -. DR EMDB; EMD-16899; -. DR EMDB; EMD-21233; -. DR EMDB; EMD-21242; -. DR EMDB; EMD-23096; -. DR EMDB; EMD-23121; -. DR EMDB; EMD-3842; -. DR EMDB; EMD-3843; -. DR EMDB; EMD-4434; -. DR SMR; Q13405; -. DR BioGRID; 107199; 183. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR CORUM; Q13405; -. DR IntAct; Q13405; 59. DR MINT; Q13405; -. DR STRING; 9606.ENSP00000279242; -. DR GlyGen; Q13405; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q13405; -. DR PhosphoSitePlus; Q13405; -. DR SwissPalm; Q13405; -. DR BioMuta; MRPL49; -. DR EPD; Q13405; -. DR jPOST; Q13405; -. DR MassIVE; Q13405; -. DR MaxQB; Q13405; -. DR PaxDb; 9606-ENSP00000279242; -. DR PeptideAtlas; Q13405; -. DR ProteomicsDB; 59387; -. DR Pumba; Q13405; -. DR TopDownProteomics; Q13405; -. DR Antibodypedia; 29687; 147 antibodies from 23 providers. DR DNASU; 740; -. DR Ensembl; ENST00000279242.7; ENSP00000279242.2; ENSG00000149792.9. DR Ensembl; ENST00000526319.5; ENSP00000434190.1; ENSG00000149792.9. DR GeneID; 740; -. DR KEGG; hsa:740; -. DR MANE-Select; ENST00000279242.7; ENSP00000279242.2; NM_004927.4; NP_004918.1. DR UCSC; uc001oda.3; human. DR AGR; HGNC:1176; -. DR CTD; 740; -. DR DisGeNET; 740; -. DR GeneCards; MRPL49; -. DR HGNC; HGNC:1176; MRPL49. DR HPA; ENSG00000149792; Low tissue specificity. DR MIM; 606866; gene. DR neXtProt; NX_Q13405; -. DR OpenTargets; ENSG00000149792; -. DR PharmGKB; PA30981; -. DR VEuPathDB; HostDB:ENSG00000149792; -. DR eggNOG; KOG4034; Eukaryota. DR GeneTree; ENSGT00390000017253; -. DR HOGENOM; CLU_085757_2_3_1; -. DR InParanoid; Q13405; -. DR OMA; NPPEWKY; -. DR OrthoDB; 2898465at2759; -. DR PhylomeDB; Q13405; -. DR TreeFam; TF317750; -. DR PathwayCommons; Q13405; -. DR Reactome; R-HSA-5368286; Mitochondrial translation initiation. DR Reactome; R-HSA-5389840; Mitochondrial translation elongation. DR Reactome; R-HSA-5419276; Mitochondrial translation termination. DR SignaLink; Q13405; -. DR SIGNOR; Q13405; -. DR BioGRID-ORCS; 740; 430 hits in 1162 CRISPR screens. DR ChiTaRS; MRPL49; human. DR GenomeRNAi; 740; -. DR Pharos; Q13405; Tbio. DR PRO; PR:Q13405; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q13405; Protein. DR Bgee; ENSG00000149792; Expressed in right adrenal gland cortex and 205 other cell types or tissues. DR ExpressionAtlas; Q13405; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB. DR GO; GO:0005761; C:mitochondrial ribosome; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR Gene3D; 3.30.780.10; SUI1-like domain; 1. DR InterPro; IPR007740; Ribosomal_mL49. DR PANTHER; PTHR13477:SF0; 39S RIBOSOMAL PROTEIN L49, MITOCHONDRIAL; 1. DR PANTHER; PTHR13477; MITOCHONDRIAL 39S RIBOSOMAL PROTEIN L49; 1. DR Pfam; PF05046; Img2; 1. DR Genevisible; Q13405; HS. PE 1: Evidence at protein level; KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1..166 FT /note="Large ribosomal subunit protein mL49" FT /id="PRO_0000207664" FT REGION 56..78 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 64..78 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 9 FT /note="T -> A (in dbSNP:rs17146691)" FT /id="VAR_021991" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 46..49 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 69..71 FT /evidence="ECO:0007829|PDB:3J7Y" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 96..101 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 105..110 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 117..132 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 138..141 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 142..145 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 154..164 FT /evidence="ECO:0007829|PDB:7OF0" SQ SEQUENCE 166 AA; 19198 MW; 66AB18FDE25D92B4 CRC64; MAATMFRATL RGWRTGVQRG CGLRLLSQTQ GPPDYPRFVE SVDEYQFVER LLPATRIPDP PKHEHYPTPS GWQPPRDPPP NLPYFVRRSR MHNIPVYKDI THGNRQMTVI RKVEGDIWAL QKDVEDFLSP LLGKTPVTQV NEVTGTLRIK GYFDQELKAW LLEKGF //