ID   RMD9_PICGU              Reviewed;         632 AA.
AC   A5DDF2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=RNA-binding protein RMD9, mitochondrial {ECO:0000250|UniProtKB:P53140};
DE   Flags: Precursor;
GN   Name=RMD9; ORFNames=PGUG_01303;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408156; EDK37205.2; -; Genomic_DNA.
DR   RefSeq; XP_001485632.1; XM_001485582.1.
DR   AlphaFoldDB; A5DDF2; -.
DR   SMR; A5DDF2; -.
DR   STRING; 4929.XP_001485632.1; -.
DR   EnsemblFungi; EDK37205; EDK37205; PGUG_01303.
DR   GeneID; 5127669; -.
DR   KEGG; pgu:PGUG_01303; -.
DR   VEuPathDB; FungiDB:PGUG_01303; -.
DR   eggNOG; ENOG502QUSW; Eukaryota.
DR   HOGENOM; CLU_019840_1_0_1; -.
DR   InParanoid; A5DDF2; -.
DR   OMA; HIYELNT; -.
DR   OrthoDB; 321092at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
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..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..632
FT                   /note="RNA-binding protein RMD9, mitochondrial"
FT                   /id="PRO_0000301787"
FT   REGION          27..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   632 AA;  73046 MW;  04864D7205AD01E7 CRC64;
     MFRLLASSGQ VSLRPVLLQH VRNNKHGLGF PNASGVPQSP SSMTSSSIVS PSQFTRSNSS
     AAGLSESPAS SVDSKIENFL SKSAKDPLVR EALDAETKNK LNYFKEQIDL AHRYRSIHDH
     DSERAFASTL DNLSRALEDE SLRDTFVSRD LFSYAQVLNS GVYNNRTNRL SGAKNRDSDQ
     YQNQNLHDEV LLKQAVLHLG ELITNGEFKA ILNAPTLSFL FYSMKQFQLY PEMIHLWENG
     VNDQQTGQVY LDEKILAVIL PVTFEQNRFT YEEILHIYEL NTEKLDKVGH ELLTSMGKIA
     IAAGDYSRGL DSLESILQLY EKAQQSHYKN KILASLSDLH LSFIGTCKDI KISKHFFDKV
     VHYDLPYRVK LKVPHIQSLL ENCYEQNEPM DNILYFWRAS IAHYNTEQQL VLNSRYAILN
     NALFTIFFKK YPELNEESFS KLREIIAMYA ESKPIDEVFL NTIIGNYSWD SKEVLEQIIE
     NYDVYNVKRT PVSYRVCLKK TGSLESYSNE EILQKWNASL KHLDENKFTY IPVADWAALR
     DATILSHFKD ARKEFYLSVL DKYKDYIQDH RSCIRFVRYW IKRKDVAADI ARVASPEPQT
     FDCDIEIQVP QFRHLRKNIN YVKEVQNMRF SG