CCM1_SCHPO
ID CCM1_SCHPO Reviewed; 687 AA.
AC O42955;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Pentatricopeptide repeat-containing protein 3, mitochondrial;
DE AltName: Full=Mitochondrial group I intron splicing factor dmr1;
DE Flags: Precursor;
GN Name=ppr3; Synonyms=dmr1; ORFNames=SPBC19G7.07c;
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: RNA-binding protein involved in the specific removal of group
CC I introns in mitochondrial encoded transcripts. Maintains the stability
CC of the small subunit mitochondrial 15S rRNA and thus the expression of
CC the mitochondrial genome. {ECO:0000269|PubMed:21727087}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:21727087}.
CC -!- DISRUPTION PHENOTYPE: Impairs growth on galactose and leads to
CC thermosensitivity on glucose-containing media.
CC {ECO:0000269|PubMed:21727087}.
CC -!- SIMILARITY: Belongs to the CCM1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17061.1; -; Genomic_DNA.
DR PIR; T39838; T39838.
DR RefSeq; NP_595973.1; NM_001021881.2.
DR AlphaFoldDB; O42955; -.
DR SMR; O42955; -.
DR BioGRID; 277247; 2.
DR STRING; 4896.SPBC19G7.07c.1; -.
DR MaxQB; O42955; -.
DR PaxDb; O42955; -.
DR EnsemblFungi; SPBC19G7.07c.1; SPBC19G7.07c.1:pep; SPBC19G7.07c.
DR GeneID; 2540724; -.
DR KEGG; spo:SPBC19G7.07c; -.
DR PomBase; SPBC19G7.07c; ppr3.
DR VEuPathDB; FungiDB:SPBC19G7.07c; -.
DR eggNOG; ENOG502QUX2; Eukaryota.
DR HOGENOM; CLU_025807_0_0_1; -.
DR InParanoid; O42955; -.
DR OMA; WHELCYQ; -.
DR PhylomeDB; O42955; -.
DR PRO; PR:O42955; -.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; 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; PF01535; PPR; 2.
DR TIGRFAMs; TIGR00756; PPR; 1.
DR PROSITE; PS51375; PPR; 4.
PE 3: Inferred from homology;
KW Mitochondrion; mRNA processing; mRNA splicing; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..49
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 50..687
FT /note="Pentatricopeptide repeat-containing protein 3,
FT mitochondrial"
FT /id="PRO_0000316605"
FT REPEAT 192..226
FT /note="PPR 1"
FT REPEAT 227..261
FT /note="PPR 2"
FT REPEAT 262..296
FT /note="PPR 3"
FT REPEAT 297..333
FT /note="PPR 4"
FT REPEAT 334..371
FT /note="PPR 5"
FT REPEAT 372..407
FT /note="PPR 6"
FT REPEAT 408..443
FT /note="PPR 7"
SQ SEQUENCE 687 AA; 79293 MW; 59B30E970ED0F77C CRC64;
MLNKCSGSLT LLAVRRFCGP CRRLHYHKDN PNNINIAKNL LNNNIQARCS TNEASWKLAQ
KELDLKIREY EQKLKDVKLN DINKKSPLNI PDEVWTKFIS EVNSYDKEKE NHLSTGNHEL
RRTTPLKIGP LLLTRIGLLK SKNTASNNYS VDHIVSNLAN DNTLLNRQVS TEEWNSHLRH
LLNIPKCFLG VDIVEIVNFF NYLPQTVISK SSLEIWKAVE ESGMKVMPDL LVLLMESTNA
SGDFRKTVQL YHLYQKSNAP PNGLVYQSYA IALSSLGKHK DLVALYSEQK SVSITPSKDF
LNACIKAFSR TKEFTKAWEV FNFMKFTATS ISPSAETYGL MIQICSSQYN PEKALDLYNE
MKLRPIDPLT PTTFVINNLI HALATDVRFQ TVAFSLLQDL SHYGLRPNHS TLYELIRLIA
YSGKLDYMKD ILDNFWVRQK LLPSILKVEQ IFHFIFRALI SAEVQTSSVT PDYTHFKEEV
RKIIDSSKEP LIPFLKRSTL TENDLFLNAI YTFEYAKRKF PEALNSRLVT DFLNIFLERG
SVQLFKEIYQ LEFREMSTME GSSMKVAKIT LTYIYAIKLA LLFNDFEFGY AAWQEYWHCK
IHKLLPKEDA SYEQKVVLLT LSLLSKNKHT SLARSLLLSH LDKGWTWNKH SLGFMRKMCS
VMNDQATVYL IDSITNEIGI NQRFTRK
