PPR32_ARATH
ID PPR32_ARATH Reviewed; 809 AA.
AC Q3E6Q1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Pentatricopeptide repeat-containing protein At1g11290, chloroplastic {ECO:0000305};
DE AltName: Full=Protein CHLORORESPIRATORY REDUCTION 22 {ECO:0000303|PubMed:19182104};
DE Flags: Precursor;
GN Name=PCMP-H40; Synonyms=CRR22 {ECO:0000303|PubMed:19182104}, PCMP-H72;
GN OrderedLocusNames=At1g11290; ORFNames=T28P6.20;
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 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 [4]
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 [5]
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).
CC -!- FUNCTION: Involved in multiple sites RNA editing events in
CC chloroplasts. Involved in the editing of the site 7 of ndhB (ndhB-7)
CC and site 5 of ndhD (ndhD-5) transcripts, which are two plastid-encoded
CC subunits of the chloroplast NAD(P)H dehydrogenase (NDH) complex.
CC Involved in the editing of the site 3 of rpoB (rpoB-3) transcript.
CC Required for the activity of the NDH complex of the photosynthetic
CC electron transport chain. Possesses low endoribonuclease activity in
CC vitro. {ECO:0000269|PubMed:19182104}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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 -!- WEB RESOURCE: Name=Pentatricopeptide repeat proteins;
CC URL="https://ppr.plantenergy.uwa.edu.au";
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DR EMBL; AC007259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE28713.1; -; Genomic_DNA.
DR RefSeq; NP_172596.1; NM_101002.2.
DR AlphaFoldDB; Q3E6Q1; -.
DR SMR; Q3E6Q1; -.
DR STRING; 3702.AT1G11290.1; -.
DR PaxDb; Q3E6Q1; -.
DR PRIDE; Q3E6Q1; -.
DR ProteomicsDB; 234859; -.
DR EnsemblPlants; AT1G11290.1; AT1G11290.1; AT1G11290.
DR GeneID; 837671; -.
DR Gramene; AT1G11290.1; AT1G11290.1; AT1G11290.
DR KEGG; ath:AT1G11290; -.
DR Araport; AT1G11290; -.
DR TAIR; locus:2202074; AT1G11290.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_002706_15_0_1; -.
DR InParanoid; Q3E6Q1; -.
DR OMA; EAWNFID; -.
DR OrthoDB; 1344243at2759; -.
DR PhylomeDB; Q3E6Q1; -.
DR PRO; PR:Q3E6Q1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q3E6Q1; baseline and differential.
DR Genevisible; Q3E6Q1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0004519; F:endonuclease activity; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; 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; -; 5.
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; 4.
DR Pfam; PF13041; PPR_2; 3.
DR Pfam; PF13812; PPR_3; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR TIGRFAMs; TIGR00756; PPR; 8.
DR PROSITE; PS51375; PPR; 15.
PE 2: Evidence at transcript level;
KW Chloroplast; mRNA processing; Plastid; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..809
FT /note="Pentatricopeptide repeat-containing protein
FT At1g11290, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000342773"
FT REPEAT 68..98
FT /note="PPR 1"
FT REPEAT 99..133
FT /note="PPR 2"
FT REPEAT 134..168
FT /note="PPR 3"
FT REPEAT 169..199
FT /note="PPR 4"
FT REPEAT 200..234
FT /note="PPR 5"
FT REPEAT 235..269
FT /note="PPR 6"
FT REPEAT 270..300
FT /note="PPR 7"
FT REPEAT 301..335
FT /note="PPR 8"
FT REPEAT 336..370
FT /note="PPR 9"
FT REPEAT 371..401
FT /note="PPR 10"
FT REPEAT 402..436
FT /note="PPR 11"
FT REPEAT 437..471
FT /note="PPR 12"
FT REPEAT 472..502
FT /note="PPR 13"
FT REPEAT 503..537
FT /note="PPR 14"
FT REPEAT 538..568
FT /note="PPR 15"
FT REPEAT 574..604
FT /note="PPR 16"
FT REGION 609..684
FT /note="Type E motif"
FT REGION 685..715
FT /note="Type E(+) motif"
FT REGION 716..809
FT /note="Type DYW motif"
SQ SEQUENCE 809 AA; 90866 MW; 682EC69783321760 CRC64;
MSSQLVQFST VPQIPNPPSR HRHFLSERNY IPANVYEHPA ALLLERCSSL KELRQILPLV
FKNGLYQEHF FQTKLVSLFC RYGSVDEAAR VFEPIDSKLN VLYHTMLKGF AKVSDLDKAL
QFFVRMRYDD VEPVVYNFTY LLKVCGDEAE LRVGKEIHGL LVKSGFSLDL FAMTGLENMY
AKCRQVNEAR KVFDRMPERD LVSWNTIVAG YSQNGMARMA LEMVKSMCEE NLKPSFITIV
SVLPAVSALR LISVGKEIHG YAMRSGFDSL VNISTALVDM YAKCGSLETA RQLFDGMLER
NVVSWNSMID AYVQNENPKE AMLIFQKMLD EGVKPTDVSV MGALHACADL GDLERGRFIH
KLSVELGLDR NVSVVNSLIS MYCKCKEVDT AASMFGKLQS RTLVSWNAMI LGFAQNGRPI
DALNYFSQMR SRTVKPDTFT YVSVITAIAE LSITHHAKWI HGVVMRSCLD KNVFVTTALV
DMYAKCGAIM IARLIFDMMS ERHVTTWNAM IDGYGTHGFG KAALELFEEM QKGTIKPNGV
TFLSVISACS HSGLVEAGLK CFYMMKENYS IELSMDHYGA MVDLLGRAGR LNEAWDFIMQ
MPVKPAVNVY GAMLGACQIH KNVNFAEKAA ERLFELNPDD GGYHVLLANI YRAASMWEKV
GQVRVSMLRQ GLRKTPGCSM VEIKNEVHSF FSGSTAHPDS KKIYAFLEKL ICHIKEAGYV
PDTNLVLGVE NDVKEQLLST HSEKLAISFG LLNTTAGTTI HVRKNLRVCA DCHNATKYIS
LVTGREIVVR DMQRFHHFKN GACSCGDYW
