ID   RMD9L_CANGA             Reviewed;         736 AA.
AC   Q6FML6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=RNA-binding protein RMD9-like, mitochondrial {ECO:0000250|UniProtKB:P53140};
DE   Flags: Precursor;
GN   OrderedLocusNames=CAGL0K07007g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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: May be involved in the processing or stability of
CC       mitochondrial mRNAs. {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; CR380957; CAG61489.1; -; Genomic_DNA.
DR   RefSeq; XP_448528.1; XM_448528.1.
DR   AlphaFoldDB; Q6FML6; -.
DR   SMR; Q6FML6; -.
DR   STRING; 284593.Q6FML6; -.
DR   PRIDE; Q6FML6; -.
DR   EnsemblFungi; CAG61489; CAG61489; CAGL0K07007g.
DR   GeneID; 2890387; -.
DR   KEGG; cgr:CAGL0K07007g; -.
DR   CGD; CAL0134107; CAGL0K07007g.
DR   VEuPathDB; FungiDB:CAGL0K07007g; -.
DR   eggNOG; ENOG502QUSW; Eukaryota.
DR   HOGENOM; CLU_019840_0_0_1; -.
DR   InParanoid; Q6FML6; -.
DR   OMA; EMKYGYL; -.
DR   Proteomes; UP000002428; Chromosome K.
DR   GO; GO:0032592; C:integral component of mitochondrial membrane; IEA:EnsemblFungi.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IEA:EnsemblFungi.
DR   GO; GO:0009060; P:aerobic respiration; IEA:EnsemblFungi.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..79
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           80..736
FT                   /note="RNA-binding protein RMD9-like, mitochondrial"
FT                   /id="PRO_0000301789"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   736 AA;  83630 MW;  0DBBFE6A2DA2D30E CRC64;
     MFRFAQPANV LKGKAPSQIV PPHPKTNSFV HPSAHPLKFN PNSAMTVEVP THQNGPASNN
     QYNGNHSRPH FKNQFSSRNS SFTNVMNYGK NHGNNNMSPD SPWYNEVVAF EDCVSQTLYM
     SQTPRRSNMR NNGNNNMNNG RRTEHPNTQA NPLFWDSIGR AMGLYHDLIN TPELNSDRVS
     KLVHLLHNGL RANRNQLTRM NKKPDYDSQS FHKEMTNYLC KSLREISEDV LNGKVELNEY
     GAMHLITAFK ELLLFQEAVN IWKSAINGSN NYTSNIFLNP RVVGVILPIL YENGVSYPEI
     QSLYEKSSSM INYFHPNLSV GMIRASLSAS ENQMALKLFQ KLCEESTEMK YGYLIETHLS
     FIGECKDLNV AQAFFDKALN DEMPYKIDLQ VSYVKSFLKN IWSQTGDFNH IYQIWYKSSL
     HYGRHVNHGI SSSLNDTFFD IFFENYANDK VQGFPMLQNI IQNYHNMKNI DEPFFNIILA
     KCTVWHDRTI LEYIDNSYDA FNIPKTIVAY RILLKSMGSI DDVTTQEILQ RWINLICKSD
     EIGQRFIANA DWAALRDATV TWTQRNRGIS SSSPMSAVNS LAPSTTNTPS PSLSPIPDRD
     TLSSARNTPN KIWSGTPVPP PSTEMDFYSH PAFQAANASG AFDDMASATV NPTPRKNFTN
     GIVPNTPQPI DDRMVLYLKI VKRYSPFCRD SRQLARLTTG TAVKYSVLQE VLNQFQSLNV
     NDIPVPELRN LKPTCV