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 13-SEP-2023, entry version 103. 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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., 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., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., 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 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 reference RT 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., Hayashizaki Y., RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., RA 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., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA 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., Le Ret M., RA Martin-Magniette M.-L., Mireau H., Peeters N., Renou J.-P., Szurek B., RA 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., Melcher K., RA 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=Pentatricopeptide repeat proteins; CC URL="https://ppr.plantenergy.uwa.edu.au"; 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 PDB; 4LEU; X-ray; 2.00 A; A=1-257. DR PDBsum; 4LEU; -. DR AlphaFoldDB; Q9STF9; -. DR SMR; Q9STF9; -. DR DIP; DIP-60556N; -. DR STRING; 3702.AT3G46870.1; -. DR PaxDb; 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; AT3G46870; -. DR eggNOG; ENOG502QPMB; Eukaryota. DR HOGENOM; CLU_077248_1_0_1; -. DR InParanoid; Q9STF9; -. DR PhylomeDB; Q9STF9; -. DR PRO; PR:Q9STF9; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9STF9; baseline and differential. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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; HDA:TAIR. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR InterPro; IPR002885; Pentatricopeptide_repeat. DR InterPro; IPR044795; THA8L-like. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR NCBIfam; TIGR00756; PPR; 2. DR PANTHER; PTHR46870; PROTEIN THYLAKOID ASSEMBLY 8-LIKE, CHLOROPLASTIC; 1. DR PANTHER; PTHR46870:SF2; PROTEIN THYLAKOID ASSEMBLY 8-LIKE, CHLOROPLASTIC; 1. DR Pfam; PF13041; PPR_2; 1. DR PROSITE; PS51375; PPR; 2. PE 1: Evidence at protein level; KW 3D-structure; Chloroplast; Plastid; Reference proteome; Repeat; KW RNA-binding; Transit peptide. FT TRANSIT 1..55 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 56..257 FT /note="Protein THYLAKOID ASSEMBLY 8-like, chloroplastic" FT /id="PRO_0000356125" FT REPEAT 142..176 FT /note="PPR 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708" FT REPEAT 177..211 FT /note="PPR 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708" FT MUTAGEN 75 FT /note="K->E: Abolished RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 86 FT /note="R->E: Reduced RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 93 FT /note="K->E: Reduced RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 96 FT /note="K->E: Reduced RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 104 FT /note="R->E: Abolished RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 119 FT /note="R->E: Abolished RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 155 FT /note="K->E: Abolished RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 157 FT /note="K->E: Reduced RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 158 FT /note="R->E: Reduced RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 186 FT /note="R->E: Reduced RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 190 FT /note="R->E: Reduced RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 206 FT /note="K->E: Reduced RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 217 FT /note="R->E: Reduced RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT MUTAGEN 221 FT /note="K->E: Reduced RNA binding." FT /evidence="ECO:0000269|PubMed:24047899" FT HELIX 75..87 FT /evidence="ECO:0007829|PDB:4LEU" FT HELIX 91..101 FT /evidence="ECO:0007829|PDB:4LEU" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:4LEU" FT HELIX 107..120 FT /evidence="ECO:0007829|PDB:4LEU" FT HELIX 123..134 FT /evidence="ECO:0007829|PDB:4LEU" FT HELIX 143..155 FT /evidence="ECO:0007829|PDB:4LEU" FT HELIX 159..171 FT /evidence="ECO:0007829|PDB:4LEU" FT HELIX 178..190 FT /evidence="ECO:0007829|PDB:4LEU" FT HELIX 194..205 FT /evidence="ECO:0007829|PDB:4LEU" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:4LEU" FT HELIX 213..222 FT /evidence="ECO:0007829|PDB:4LEU" FT TURN 223..225 FT /evidence="ECO:0007829|PDB:4LEU" FT HELIX 227..240 FT /evidence="ECO:0007829|PDB:4LEU" FT HELIX 242..247 FT /evidence="ECO:0007829|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 //