ID   RMD9_LODEL              Reviewed;         623 AA.
AC   A5E057;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=RNA-binding protein RMD9, mitochondrial {ECO:0000250|UniProtKB:P53140};
DE   Flags: Precursor;
GN   Name=RMD9; ORFNames=LELG_02994;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
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; CH981526; EDK44815.1; -; Genomic_DNA.
DR   RefSeq; XP_001526436.1; XM_001526386.1.
DR   AlphaFoldDB; A5E057; -.
DR   SMR; A5E057; -.
DR   STRING; 379508.A5E057; -.
DR   EnsemblFungi; EDK44815; EDK44815; LELG_02994.
DR   GeneID; 5233133; -.
DR   KEGG; lel:LELG_02994; -.
DR   VEuPathDB; FungiDB:LELG_02994; -.
DR   eggNOG; ENOG502QUSW; Eukaryota.
DR   HOGENOM; CLU_019840_1_0_1; -.
DR   InParanoid; A5E057; -.
DR   OMA; HIYELNT; -.
DR   OrthoDB; 321092at2759; -.
DR   Proteomes; UP000001996; 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..60
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           61..623
FT                   /note="RNA-binding protein RMD9, mitochondrial"
FT                   /id="PRO_0000301786"
FT   REGION          20..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  71238 MW;  16BA74A2B4033348 CRC64;
     MFRLVNTSQG LRPALISKFK HAKTGGTNPS PFSTTTTNAP TNTTPTSNSK YESTFQFKRA
     QSTVAPPATV ATTIQTPSSQ NAAANPYRSK LDSFSRIYHV PNHVVGRRTE KIDHTATDEM
     ATLILDENFR NQMTETDLYR YAASIYSAAI AVRRQRLEMS RNRDRDNAAS FGDDLKYQSA
     AIALAESIAA GEFPQQVSAR TLFKVFATLM QFKLNDEIMN LWETGVAQSE GEDLGDIGKM
     YLDHTVLSVV LEVAYDSKRF SYEEILRIYE MSLVENEPIH PYLLERIGQI AIKHGDHARG
     LDCLEQLMNN YENNPRARSI LGALSQIHIA FIGNCKDTII AKRFFEKAVD ESDHLPYTIL
     LKAPYVVSFL QNCNALGDSF ENIVDMWSRV CQFYIKRREE QPSRMVTINS GLFKILFDKY
     PEPSMEAMKL MKLTFAKCKN INEHFLNTLI SHMPWKDRTL VNDVVSAYDK FKVPKSVVSH
     RIILKNAGNV EYTPEEILTL WNQLLLKLDS EGYKYIANAD WAAIRLATIF SEQFKSPERD
     CLYYSIVRTY KNYMQHDEAA LRFLRATVRD ATVYKQISRI TTEENPTFEI NYDIEVPEFK
     NLKENTNYPK VTKKVTDANP NLL