PPR85_ARATH
ID PPR85_ARATH Reviewed; 638 AA.
AC Q0WQW5; Q9LQ42; Q9XIF6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Pentatricopeptide repeat-containing protein At1g59720, chloroplastic/mitochondrial {ECO:0000305};
DE AltName: Full=Protein CHLORORESPIRATORY REDUCTION 28 {ECO:0000303|PubMed:19182104};
DE Flags: Precursor;
GN Name=PCMP-H51; Synonyms=CRR28 {ECO:0000303|PubMed:19182104};
GN OrderedLocusNames=At1g59720; ORFNames=F23H11.3, T30E16.32;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] OF 10-638.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY.
RX PubMed=10809006; DOI=10.1023/a:1006352315928;
RA Aubourg S., Boudet N., Kreis M., Lecharny A.;
RT "In Arabidopsis thaliana, 1% of the genome codes for a novel protein family
RT unique to plants.";
RL Plant Mol. Biol. 42:603-613(2000).
RN [5]
RP GENE FAMILY, AND SUBCELLULAR LOCATION.
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19182104; DOI=10.1105/tpc.108.064667;
RA Okuda K., Chateigner-Boutin A.L., Nakamura T., Delannoy E., Sugita M.,
RA Myouga F., Motohashi R., Shinozaki K., Small I., Shikanai T.;
RT "Pentatricopeptide repeat proteins with the DYW motif have distinct
RT molecular functions in RNA editing and RNA cleavage in Arabidopsis
RT chloroplasts.";
RL Plant Cell 21:146-156(2009).
RN [7]
RP INTERACTION WITH ORRM1.
RX PubMed=23487777; DOI=10.1073/pnas.1220162110;
RA Sun T., Germain A., Giloteaux L., Hammani K., Barkan A., Hanson M.R.,
RA Bentolila S.;
RT "An RNA recognition motif-containing protein is required for plastid RNA
RT editing in Arabidopsis and maize.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E1169-E1178(2013).
RN [8]
RP INTERACTION WITH VAR3/OZ1.
RX PubMed=25768119; DOI=10.1371/journal.pgen.1005028;
RA Sun T., Shi X., Friso G., Van Wijk K., Bentolila S., Hanson M.R.;
RT "A zinc finger motif-containing protein is essential for chloroplast RNA
RT editing.";
RL PLoS Genet. 11:E1005028-E1005028(2015).
CC -!- FUNCTION: Involved in multiple sites RNA editing events in
CC chloroplasts. Involved in the editing of the site 2 of ndhB (ndhB-2)
CC and site 3 of ndhD (ndhD-3) transcripts, which are two plastid-encoded
CC subunits of the chloroplast NAD(P)H dehydrogenase (NDH) complex.
CC Required for the activity of the NDH complex of the photosynthetic
CC electron transport chain. {ECO:0000269|PubMed:19182104}.
CC -!- SUBUNIT: Interacts with ORRM1 (PubMed:23487777). Interacts with
CC VAR3/OZ1 (PubMed:25768119). {ECO:0000269|PubMed:23487777,
CC ECO:0000269|PubMed:25768119}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. Mitochondrion
CC {ECO:0000269|PubMed:15269332}.
CC -!- DISRUPTION PHENOTYPE: Impaired chloroplastic NAD(P)H dehydrogenase
CC (NDH) activity. {ECO:0000269|PubMed:19182104}.
CC -!- MISCELLANEOUS: The DYW motif is dispensable for editing activity in
CC vivo. {ECO:0000269|PubMed:19182104}.
CC -!- SIMILARITY: Belongs to the PPR family. PCMP-H subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39314.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF79766.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Pentatricopeptide repeat proteins;
CC URL="https://ppr.plantenergy.uwa.edu.au";
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DR EMBL; AC007258; AAD39314.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC009317; AAF79766.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33607.1; -; Genomic_DNA.
DR EMBL; AK228565; BAF00484.1; -; mRNA.
DR PIR; H96620; H96620.
DR RefSeq; NP_176180.1; NM_104664.2.
DR AlphaFoldDB; Q0WQW5; -.
DR SMR; Q0WQW5; -.
DR BioGRID; 27488; 1.
DR STRING; 3702.AT1G59720.1; -.
DR PaxDb; Q0WQW5; -.
DR PRIDE; Q0WQW5; -.
DR ProteomicsDB; 234861; -.
DR EnsemblPlants; AT1G59720.1; AT1G59720.1; AT1G59720.
DR GeneID; 842263; -.
DR Gramene; AT1G59720.1; AT1G59720.1; AT1G59720.
DR KEGG; ath:AT1G59720; -.
DR Araport; AT1G59720; -.
DR TAIR; locus:2025946; AT1G59720.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_002706_37_2_1; -.
DR InParanoid; Q0WQW5; -.
DR OMA; HFYATCG; -.
DR OrthoDB; 1344243at2759; -.
DR PhylomeDB; Q0WQW5; -.
DR PRO; PR:Q0WQW5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WQW5; baseline and differential.
DR Genevisible; Q0WQW5; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016556; P:mRNA modification; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR032867; DYW_dom.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF14432; DYW_deaminase; 1.
DR Pfam; PF01535; PPR; 1.
DR Pfam; PF13041; PPR_2; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR TIGRFAMs; TIGR00756; PPR; 4.
DR PROSITE; PS51375; PPR; 10.
PE 1: Evidence at protein level;
KW Chloroplast; Mitochondrion; mRNA processing; Plastid; Reference proteome;
KW Repeat; Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast and mitochondrion"
FT CHAIN 41..638
FT /note="Pentatricopeptide repeat-containing protein
FT At1g59720, chloroplastic/mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000342826"
FT REPEAT 82..112
FT /note="PPR 1"
FT REPEAT 113..148
FT /note="PPR 2"
FT REPEAT 150..184
FT /note="PPR 3"
FT REPEAT 185..215
FT /note="PPR 4"
FT REPEAT 216..246
FT /note="PPR 5"
FT REPEAT 250..280
FT /note="PPR 6"
FT REPEAT 288..318
FT /note="PPR 7"
FT REPEAT 319..353
FT /note="PPR 8"
FT REPEAT 356..390
FT /note="PPR 9"
FT REPEAT 392..422
FT /note="PPR 10"
FT REGION 427..510
FT /note="Type E motif"
FT REGION 511..541
FT /note="Type E(+) motif"
FT REGION 542..638
FT /note="Type DYW motif"
SQ SEQUENCE 638 AA; 71960 MW; B868192817B41756 CRC64;
MVVRSIIVSP PTTITYYHPM SIGLLVHPLS PHIPPASSPS ASTAGNHHQR IFSLAETCSD
MSQLKQLHAF TLRTTYPEEP ATLFLYGKIL QLSSSFSDVN YAFRVFDSIE NHSSFMWNTL
IRACAHDVSR KEEAFMLYRK MLERGESSPD KHTFPFVLKA CAYIFGFSEG KQVHCQIVKH
GFGGDVYVNN GLIHLYGSCG CLDLARKVFD EMPERSLVSW NSMIDALVRF GEYDSALQLF
REMQRSFEPD GYTMQSVLSA CAGLGSLSLG TWAHAFLLRK CDVDVAMDVL VKNSLIEMYC
KCGSLRMAEQ VFQGMQKRDL ASWNAMILGF ATHGRAEEAM NFFDRMVDKR ENVRPNSVTF
VGLLIACNHR GFVNKGRQYF DMMVRDYCIE PALEHYGCIV DLIARAGYIT EAIDMVMSMP
MKPDAVIWRS LLDACCKKGA SVELSEEIAR NIIGTKEDNE SSNGNCSGAY VLLSRVYASA
SRWNDVGIVR KLMSEHGIRK EPGCSSIEIN GISHEFFAGD TSHPQTKQIY QQLKVIDDRL
RSIGYLPDRS QAPLVDATND GSKEYSLRLH SERLAIAFGL INLPPQTPIR IFKNLRVCND
CHEVTKLISK VFNTEIIVRD RVRFHHFKDG SCSCLDYW
