PPR5_MAIZE
ID PPR5_MAIZE Reviewed; 499 AA.
AC A7LN87; C0P2Q7;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Pentatricopeptide repeat-containing protein PPR5, chloroplastic {ECO:0000305};
DE AltName: Full=Pentatricopeptide repeat-containing protein 5 {ECO:0000303|PubMed:18591259};
DE Short=ZmPPR5 {ECO:0000303|PubMed:18591259};
DE Flags: Precursor;
GN Name=PPR5 {ECO:0000303|PubMed:18591259};
GN ORFNames=ZEAMMB73_Zm00001d052240 {ECO:0000312|EMBL:AQK56524.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. B73;
RX PubMed=18591259; DOI=10.1128/mcb.00563-08;
RA Beick S., Schmitz-Linneweber C., Williams-Carrier R., Jensen B., Barkan A.;
RT "The pentatricopeptide repeat protein PPR5 stabilizes a specific tRNA
RT precursor in maize chloroplasts.";
RL Mol. Cell. Biol. 28:5337-5347(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 110-499.
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [4]
RP FUNCTION.
RX PubMed=18669444; DOI=10.1261/rna.1077708;
RA Williams-Carrier R., Kroeger T., Barkan A.;
RT "Sequence-specific binding of a chloroplast pentatricopeptide repeat
RT protein to its native group II intron ligand.";
RL RNA 14:1930-1941(2008).
CC -!- FUNCTION: Involved in the biogenesis of the plastid translation
CC machinery by promoting the splicing of group II introns in
CC chloroplasts. Stabilizes the chloroplast trnG pre-RNA by directly
CC binding to a group II intron, where it protects an endonuclease-
CC sensitive site and stimulates splicing (PubMed:18591259). Binds
CC specific sites within group II intron trnG pre-RNA. Binds with high
CC affinity to the 5'-UTR of the chloroplastic petA mRNA
CC (PubMed:18669444). {ECO:0000269|PubMed:18591259,
CC ECO:0000269|PubMed:18669444}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Albino or pale green seedlings. Seedling
CC lethality. {ECO:0000269|PubMed:18591259}.
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
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DR EMBL; EU037901; ABS82814.1; -; mRNA.
DR EMBL; CM000780; AQK56524.1; -; Genomic_DNA.
DR EMBL; BT062576; ACN27273.1; -; mRNA.
DR RefSeq; NP_001106062.1; NM_001112592.1.
DR AlphaFoldDB; A7LN87; -.
DR SMR; A7LN87; -.
DR STRING; 4577.GRMZM2G025409_P01; -.
DR PaxDb; A7LN87; -.
DR PRIDE; A7LN87; -.
DR GeneID; 100126361; -.
DR KEGG; zma:100126361; -.
DR eggNOG; KOG4197; Eukaryota.
DR OMA; ITYECLI; -.
DR OrthoDB; 1344243at2759; -.
DR Proteomes; UP000007305; Chromosome 4.
DR ExpressionAtlas; A7LN87; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0031425; P:chloroplast RNA processing; IMP:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR GO; GO:0000373; P:Group II intron splicing; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR044179; PPR5-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR47874; PTHR47874; 1.
DR Pfam; PF01535; PPR; 2.
DR Pfam; PF13041; PPR_2; 2.
DR Pfam; PF13812; PPR_3; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR TIGRFAMs; TIGR00756; PPR; 6.
DR PROSITE; PS51375; PPR; 9.
PE 2: Evidence at transcript level;
KW Chloroplast; mRNA processing; mRNA splicing; Plastid; Reference proteome;
KW Repeat; RNA-binding; Transit peptide; Translation regulation.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..499
FT /note="Pentatricopeptide repeat-containing protein PPR5,
FT chloroplastic"
FT /id="PRO_0000441902"
FT REPEAT 123..157
FT /note="PPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 158..193
FT /note="PPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 198..232
FT /note="PPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 233..267
FT /note="PPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 268..302
FT /note="PPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 303..337
FT /note="PPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 338..372
FT /note="PPR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 373..407
FT /note="PPR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 408..442
FT /note="PPR 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 55936 MW; 0C32EBCCA17F8069 CRC64;
MLACPSTSSP WPQRQPPSPC PGGGGGATRH VALAARSKRR GAGPAAAEGV DEAAAEAAEL
VRSLLRRTAG GKERLVPVLD RHVRVVRTEH CFLLFEELGR RDAWLQCLDV FRWMQKQRWY
VADNGIYSKL ISVMGRKGQI RMAMWLFSQM RNSGCKPDTS VYNSLIGAHL HSRDKTKALA
KALGYFEKMK CIERCQPTIV TYNILLRAFA QAGDTKQVDM LFKDLDESVV SPDVYTYNGV
LDAYGKNGMI KEMESVLVRM KSTQCRPDVI TFNILIDSYG RKQTFDKMEQ VFKSLLRSKE
RPTHPTFNSM ITNYGRARLR EKAESVVEKM EELGFKPNYV TQECLIIMYA HCDCVSKARQ
VFDELVTSQT KVHLSSLNSM LEAYCMNGLH TEADRLLDTA LQQCVVPNGS TYKLLYKAYT
KANDKLLVQK LLKRMNKQGI VPNKKFFLDA LEAFGTSDRK PRTSPGINSA SKPSTDSAGD
SETATSDKPE VSVWHVAAT
