PPR2_SCHPO
ID PPR2_SCHPO Reviewed; 432 AA.
AC O60142;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Pentatricopeptide repeat-containing protein 2, mitochondrial;
DE Flags: Precursor;
GN Name=ppr2; ORFNames=SPBC18H10.11c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP DOMAIN, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21727087; DOI=10.1093/nar/gkr511;
RA Kuhl I., Dujeancourt L., Gaisne M., Herbert C.J., Bonnefoy N.;
RT "A genome wide study in fission yeast reveals nine PPR proteins that
RT regulate mitochondrial gene expression.";
RL Nucleic Acids Res. 39:8029-8041(2011).
CC -!- FUNCTION: Mitochondrial RNA-binding protein that acts as a general
CC translation factor. {ECO:0000269|PubMed:21727087}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:21727087}.
CC -!- DISRUPTION PHENOTYPE: Impairs growth on galactose.
CC {ECO:0000269|PubMed:21727087}.
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DR EMBL; CU329671; CAA18408.1; -; Genomic_DNA.
DR PIR; T39775; T39775.
DR RefSeq; NP_595735.1; NM_001021633.2.
DR AlphaFoldDB; O60142; -.
DR SMR; O60142; -.
DR BioGRID; 277316; 86.
DR STRING; 4896.SPBC18H10.11c.1; -.
DR MaxQB; O60142; -.
DR PaxDb; O60142; -.
DR PRIDE; O60142; -.
DR EnsemblFungi; SPBC18H10.11c.1; SPBC18H10.11c.1:pep; SPBC18H10.11c.
DR GeneID; 2540797; -.
DR KEGG; spo:SPBC18H10.11c; -.
DR PomBase; SPBC18H10.11c; ppr2.
DR VEuPathDB; FungiDB:SPBC18H10.11c; -.
DR eggNOG; ENOG502QSY4; Eukaryota.
DR HOGENOM; CLU_625787_0_0_1; -.
DR InParanoid; O60142; -.
DR OMA; ASADFYW; -.
DR PhylomeDB; O60142; -.
DR PRO; PR:O60142; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0140053; P:mitochondrial gene expression; IMP:PomBase.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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; 1.
DR PROSITE; PS51375; PPR; 2.
PE 4: Predicted;
KW Activator; Mitochondrion; Protein biosynthesis; Reference proteome; Repeat;
KW Transit peptide; Translation regulation.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..432
FT /note="Pentatricopeptide repeat-containing protein 2,
FT mitochondrial"
FT /id="PRO_0000316604"
FT REPEAT 108..142
FT /note="PPR 1"
FT REPEAT 143..179
FT /note="PPR 2"
FT REPEAT 360..394
FT /note="PPR 3"
FT REPEAT 395..429
FT /note="PPR 4"
SQ SEQUENCE 432 AA; 50048 MW; C395CB5D16C6AE5B CRC64;
MQFIKRTFPR RAFVDLLLNR FCLREFATTY SVSVSNARKL VRKRLLIADA LKFKEQVNNL
NEFRNKKTKS SLIRNDGFKL AKNVSSLLQK ESLEKALHLL YERSNAKKTV AYNLVLQYHL
AKGHYNAAWS LYNDMKKRQQ KPSDHTYSIL LKGFCDAIEK NKQGNFSKLR EYSEKVTASA
LKESNNVTSN LHHIRIISKC SLKLKSMVLV SMIIPSIKQT LDFYSGSQIL RLLNDFSMFN
PEQREEVLKM GTNLWNYFVL ECQKKGIAVD ESLICSFVKL LATSNSPQVR NVGLNILTKV
MGLEYQIFED SNLRYPLPPY CDCTSRSLVT ALQVIRQIQN GDLLARYWKY FEESHKFDLN
LQVYHEKLRN LVQQGQAAEC LNTIKRMSHN GPFPTQQTFL IVLSLCKRPK FYSYTKSFLD
LAKKLNVPVE AT
