ID THA8L_ARATH Reviewed; 257 AA. AC Q9STF9; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 16-JAN-2019, entry version 84. DE RecName: Full=Protein THYLAKOID ASSEMBLY 8-like, chloroplastic {ECO:0000303|PubMed:24047899}; DE Short=AtTHA8L {ECO:0000303|PubMed:24047899}; DE Flags: Precursor; GN Name=THA8L {ECO:0000303|PubMed:24047899}; GN OrderedLocusNames=At3g46870 {ECO:0000312|Araport:AT3G46870}; GN ORFNames=T6H20.100 {ECO:0000312|EMBL:CAB51178.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis RT thaliana."; RL Nature 408:820-822(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana RT reference genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=11910074; DOI=10.1126/science.1071006; RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., RA Shibata K., Shinagawa A., Shinozaki K.; RT "Functional annotation of a full-length Arabidopsis cDNA collection."; RL Science 296:141-145(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP GENE FAMILY. RX PubMed=15269332; DOI=10.1105/tpc.104.022236; RA Lurin C., Andres C., Aubourg S., Bellaoui M., Bitton F., Bruyere C., RA Caboche M., Debast C., Gualberto J., Hoffmann B., Lecharny A., RA Le Ret M., Martin-Magniette M.-L., Mireau H., Peeters N., Renou J.-P., RA Szurek B., Taconnat L., Small I.; RT "Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins RT reveals their essential role in organelle biogenesis."; RL Plant Cell 16:2089-2103(2004). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, AND MUTAGENESIS OF RP LYS-75; ARG-86; LYS-93; LYS-96; ARG-104; ARG-119; LYS-155; LYS-157; RP ARG-158; ARG-186; ARG-190; LYS-206; ARG-217 AND LYS-221. RX PubMed=24047899; DOI=10.1074/jbc.M113.496828; RA Ban T., Ke J., Chen R., Gu X., Tan M.H.E., Zhou X.E., Kang Y., RA Melcher K., Zhu J.-K., Xu H.E.; RT "Structure of a PLS-class pentatricopeptide repeat protein provides RT insights into mechanism of RNA recognition."; RL J. Biol. Chem. 288:31540-31548(2013). CC -!- FUNCTION: Binds weakly to specific single strand RNA (ssRNA). CC {ECO:0000269|PubMed:24047899}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. CC -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Arabidopsis PPR Protein Database; CC URL="http://www.plantenergy.uwa.edu.au/applications/ppr/ppr.php"; 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; AL096859; CAB51178.1; -; Genomic_DNA. DR EMBL; CP002686; AEE78213.1; -; Genomic_DNA. DR EMBL; AK117833; BAC42475.1; -; mRNA. DR EMBL; BT005267; AAO63331.1; -; mRNA. DR PIR; T12961; T12961. DR RefSeq; NP_190271.1; NM_114554.4. DR UniGene; At.35875; -. DR PDB; 4LEU; X-ray; 2.00 A; A=1-257. DR PDBsum; 4LEU; -. DR ProteinModelPortal; Q9STF9; -. DR SMR; Q9STF9; -. DR DIP; DIP-60556N; -. DR PaxDb; Q9STF9; -. DR PRIDE; Q9STF9; -. DR EnsemblPlants; AT3G46870.1; AT3G46870.1; AT3G46870. DR GeneID; 823840; -. DR Gramene; AT3G46870.1; AT3G46870.1; AT3G46870. DR KEGG; ath:AT3G46870; -. DR Araport; AT3G46870; -. DR TAIR; locus:2102832; AT3G46870. DR eggNOG; ENOG410II8U; Eukaryota. DR eggNOG; ENOG410YDVV; LUCA. DR HOGENOM; HOG000244234; -. DR InParanoid; Q9STF9; -. DR OrthoDB; 1211396at2759; -. DR PhylomeDB; Q9STF9; -. DR PRO; PR:Q9STF9; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9STF9; baseline and differential. DR GO; GO:0009507; C:chloroplast; IDA:TAIR. DR GO; GO:1990825; F:sequence-specific mRNA binding; IDA:UniProtKB. DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:TAIR. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR002885; Pentatricopeptide_repeat. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR Pfam; PF13041; PPR_2; 1. DR TIGRFAMs; TIGR00756; PPR; 2. DR PROSITE; PS51375; PPR; 2. PE 1: Evidence at protein level; KW 3D-structure; Chloroplast; Complete proteome; Plastid; KW Reference proteome; Repeat; RNA-binding; Transit peptide. FT TRANSIT 1 55 Chloroplast. {ECO:0000255}. FT CHAIN 56 257 Protein THYLAKOID ASSEMBLY 8-like, FT chloroplastic. FT /FTId=PRO_0000356125. FT REPEAT 142 176 PPR 1. {ECO:0000255|PROSITE- FT ProRule:PRU00708}. FT REPEAT 177 211 PPR 2. {ECO:0000255|PROSITE- FT ProRule:PRU00708}. FT MUTAGEN 75 75 K->E: Abolished RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 86 86 R->E: Reduced RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 93 93 K->E: Reduced RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 96 96 K->E: Reduced RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 104 104 R->E: Abolished RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 119 119 R->E: Abolished RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 155 155 K->E: Abolished RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 157 157 K->E: Reduced RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 158 158 R->E: Reduced RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 186 186 R->E: Reduced RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 190 190 R->E: Reduced RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 206 206 K->E: Reduced RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 217 217 R->E: Reduced RNA binding. FT {ECO:0000269|PubMed:24047899}. FT MUTAGEN 221 221 K->E: Reduced RNA binding. FT {ECO:0000269|PubMed:24047899}. FT HELIX 75 87 {ECO:0000244|PDB:4LEU}. FT HELIX 91 101 {ECO:0000244|PDB:4LEU}. FT TURN 102 104 {ECO:0000244|PDB:4LEU}. FT HELIX 107 120 {ECO:0000244|PDB:4LEU}. FT HELIX 123 134 {ECO:0000244|PDB:4LEU}. FT HELIX 143 155 {ECO:0000244|PDB:4LEU}. FT HELIX 159 171 {ECO:0000244|PDB:4LEU}. FT HELIX 178 190 {ECO:0000244|PDB:4LEU}. FT HELIX 194 205 {ECO:0000244|PDB:4LEU}. FT STRAND 207 209 {ECO:0000244|PDB:4LEU}. FT HELIX 213 222 {ECO:0000244|PDB:4LEU}. FT TURN 223 225 {ECO:0000244|PDB:4LEU}. FT HELIX 227 240 {ECO:0000244|PDB:4LEU}. FT HELIX 242 247 {ECO:0000244|PDB:4LEU}. SQ SEQUENCE 257 AA; 30133 MW; C6D3D8189362F7F7 CRC64; MTAIRVCSRK FPTFASIFFQ NITRNPSIHR ISFSNLKPKT LLHPIPPKPF TVFVSRFHDG RPRGPLWRGK KLIGKEALFV ILGLKRLKED DEKLDKFIKT HVFRLLKLDM LAVIGELERQ EETALAIKMF EVIQKQEWYQ PDVFMYKDLI VSLAKSKRMD EAMALWEKMK KENLFPDSQT YTEVIRGFLR DGCPADAMNV YEDMLKSPDP PEELPFRVLL KGLLPHPLLR NKVKKDFEEL FPEKHAYDPP EEIFGRC //