ID   RMD9_ASHGO              Reviewed;         667 AA.
AC   Q754V0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=RNA-binding protein RMD9, mitochondrial {ECO:0000250|UniProtKB:P53140};
DE   Flags: Precursor;
GN   Name=RMD9; OrderedLocusNames=AFL029W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Binds the 3'-UTR of mitochondrial mRNAs. Involved in the
CC       processing or stability of mitochondrial mRNAs.
CC       {ECO:0000250|UniProtKB:P53140}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P53140}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P53140}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P53140}; Matrix side
CC       {ECO:0000250|UniProtKB:P53140}.
CC   -!- PTM: Phosphorylated. Phosphorylation promotes binding to RNA.
CC       {ECO:0000250|UniProtKB:P53140}.
CC   -!- SIMILARITY: Belongs to the RMD9 family. {ECO:0000305}.
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DR   EMBL; AE016819; AAS53343.1; -; Genomic_DNA.
DR   RefSeq; NP_985519.1; NM_210873.1.
DR   AlphaFoldDB; Q754V0; -.
DR   SMR; Q754V0; -.
DR   STRING; 33169.AAS53343; -.
DR   EnsemblFungi; AAS53343; AAS53343; AGOS_AFL029W.
DR   GeneID; 4621752; -.
DR   KEGG; ago:AGOS_AFL029W; -.
DR   eggNOG; ENOG502QUSW; Eukaryota.
DR   HOGENOM; CLU_019840_0_0_1; -.
DR   InParanoid; Q754V0; -.
DR   OMA; EMKYGYL; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Reference proteome; Sporulation; Transit peptide.
FT   TRANSIT         1..12
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           13..667
FT                   /note="RNA-binding protein RMD9, mitochondrial"
FT                   /id="PRO_0000301781"
SQ   SEQUENCE   667 AA;  74874 MW;  F9CE131F22AFFB8B CRC64;
     MFRFVQQSQL RKAWVPNQLV SASRNSLHAQ NSLRFNSAAA VERTAETVGG GANGYGGSGD
     AGAPLDRAVN KVRSMRRGFK LGKSFPKPPS PESPWYHKVC AFDEYVASSL NAGNETGSAG
     WAKSQRATMF WDSITKAMNL YRELLLSQEL TQARVSRLLS LLHLALKINR SNMTGLNKKP
     DYDSQSFHKT MTNYLYASFK EISQDVLNGQ VTVAHVGAFH LLESFRELLL AEEAVLLWRT
     ATASEKPGLV APFMHPDPVG IMLPLLHEGG MTFEEVSALY EKCKKGQNPT ALHCLTLGMI
     KVCLSAGANA EAVGLFQEIC SLPGNSVSKA TLTGIHLAFI GECKDLQLAT VFFNRALSGE
     TPYKMNIHVS SVKQLLQNIW DQTEDFEQVF DVWRRASNYY VGLSSQGIFS SLNSKFFEIF
     FQKYRNDKVA GMQHLMEIIT GYNEIRSVDE PFLNIILTKC VVWKDLEIIE NIEESYQIYQ
     LSKSIVSCRI LLKAMGCVEV SNEQIYSRWL RLVQKADQIG QTYIANADWA ALRDATVGYI
     HQNQKEEHAD SPENLATSYP DYNPALEAAN ASGAFDSDLP FGEHGNAIKK HIIATDDRSE
     LYFRMVKKFG QYCRDSKQLV RITRGITESY PFTKEYSDNF MSMDVSDIQM PKLVNLRSKS
     QLFASYF