ID   RMD9_KLULA              Reviewed;         664 AA.
AC   Q6CKI3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=RNA-binding protein RMD9, mitochondrial {ECO:0000250|UniProtKB:P53140};
DE   Flags: Precursor;
GN   Name=RMD9; OrderedLocusNames=KLLA0F10461g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98264.1; -; Genomic_DNA.
DR   RefSeq; XP_455556.1; XM_455556.1.
DR   AlphaFoldDB; Q6CKI3; -.
DR   SMR; Q6CKI3; -.
DR   STRING; 28985.XP_455556.1; -.
DR   EnsemblFungi; CAG98264; CAG98264; KLLA0_F10461g.
DR   GeneID; 2895723; -.
DR   KEGG; kla:KLLA0_F10461g; -.
DR   eggNOG; ENOG502QUSW; Eukaryota.
DR   HOGENOM; CLU_019840_0_0_1; -.
DR   InParanoid; Q6CKI3; -.
DR   OMA; EMKYGYL; -.
DR   Proteomes; UP000000598; 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..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..664
FT                   /note="RNA-binding protein RMD9, mitochondrial"
FT                   /id="PRO_0000301785"
FT   REGION          38..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   664 AA;  75244 MW;  95D7CBA131169731 CRC64;
     MFRLVQQQTL KSRVPNQFVS ASRNSLNSQF RFNSAVALER NPQQDPTTAA PAKSSSDKRN
     SKKKYENNEI IERNVKKVRN LRRNIKFDNF KNSPNSPAFS KLNALDDCLA RGLEASSSRA
     PDGKFLDQSS LFWDSVSSSM NIYRELVITG DLNNHRASRV IQLMHVALKV NRTQLTSMNK
     KPDYDSQSFH KEMTNYLCES LREISGDILA NRVSVSEHGA AHLLSSFKEL LLYEETLNIW
     KAAVNSENKD IVKSFMFPNV VGVVLPLLYE NGTTFEEIKK LYEKSASNTT RSHGSPSLVL
     GMIKTSLAAN ENEHALSLFQ EMCTSEGFGV SPYAVLTGTH LAFIGECKDL YVAKSFFERA
     LSKDMPYKIN LQVSSVKQLI QNIWDQTHDF NEVVDVWTKA TKYYGKDVSH GISSSLNSKF
     ISIFFENYVT DKAAGLQHLQ ELVTAYDEMK AIDEPFLNII LTKCTVWQDR NIIESIEKSY
     ELYHIPKTIV TYRIILKAMG SISVPNDVIR EKWVQLIQKA DQIGQTYIAN ADWAALRDAT
     VTYTQEQFKN GGSYEMTTSD SYNPALEAAN ASGAFDDFNE PTSGTKHADH LNTQTNKEDN
     DRILLYYQLV KRYGVYCRDP KQYARITSGI ALNFEVAQPY LGLVNTMDVS SIYVPPLRNF
     HLNH