ID   RMD9_DEBHA              Reviewed;         622 AA.
AC   Q6BML3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=RNA-binding protein RMD9, mitochondrial {ECO:0000250|UniProtKB:P53140};
DE   Flags: Precursor;
GN   Name=RMD9; OrderedLocusNames=DEHA2F04422g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382138; CAG88876.2; -; Genomic_DNA.
DR   RefSeq; XP_460558.2; XM_460558.1.
DR   AlphaFoldDB; Q6BML3; -.
DR   SMR; Q6BML3; -.
DR   STRING; 4959.XP_460558.2; -.
DR   EnsemblFungi; CAG88876; CAG88876; DEHA2F04422g.
DR   GeneID; 2903216; -.
DR   KEGG; dha:DEHA2F04422g; -.
DR   eggNOG; ENOG502QUSW; Eukaryota.
DR   HOGENOM; CLU_019840_1_0_1; -.
DR   InParanoid; Q6BML3; -.
DR   OMA; HIYELNT; -.
DR   OrthoDB; 321092at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
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..108
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           109..622
FT                   /note="RNA-binding protein RMD9, mitochondrial"
FT                   /id="PRO_0000301784"
SQ   SEQUENCE   622 AA;  71875 MW;  9C5B0CB7EDF711FD CRC64;
     MFRLLSANTQ QTLRPAILSK VRSNKANISL PSSSIQVNPP SPAQYNLTCQ FTRHNSSASS
     QKTKSSKVDA FVNKAQRDPV LREALDSEAN SKLNYFKEQL SLAFQYRSAK DRDSQRAFVA
     TVDNLFKAFE DESLRSSYSS RDLYSYTQIL NFSVYHNRTN RLSSSRNRDS DQYQNENLHD
     EVLIKSAVLN LSETIISGEF NKILNANILS YLFYSMKQFQ LYPEMLNLWE NGVNDGETGK
     LFLNEKILAV ILPIAYEQKR FSYEEILHIY ELNTKELSTV QHELLCSIGK IAIGSGDYSR
     GLDSLEALLQ LYESKQQSTQ HVLASLGELH LNFIGSCKDI KISKHFFDKV VQYDLPYYVC
     LKVPYIQSLL QNCFELNESL DNIIYFWKST ITHYSNEKNS AGLNSRYSIL NNTFFTIFFK
     IYPTLNAESF NKLREVIALY AEIKPVDEVF LNTIIGNYSW GDKNVLEQLI ENYSIYNVKR
     TPVSYRICLK KTGELPQYTN EDILIKWNDS LQHLDQNGFN YIPIADWAAL RDATILSNSG
     SDRKDFYLAV ANQYKDYIQD QRSCIRFVKY WLKKREHLKS FSTLTFGSDA DFSNEVDIVV
     PQFRHLKPNI NYQKISSKII GK