ID   RMD9_PICST              Reviewed;         629 AA.
AC   A3LQ52;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=RNA-binding protein RMD9, mitochondrial {ECO:0000250|UniProtKB:P53140};
DE   Flags: Precursor;
GN   Name=RMD9; ORFNames=PICST_88098;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000496; ABN65153.2; -; Genomic_DNA.
DR   RefSeq; XP_001383182.2; XM_001383145.1.
DR   AlphaFoldDB; A3LQ52; -.
DR   SMR; A3LQ52; -.
DR   STRING; 4924.XP_001383182.2; -.
DR   PRIDE; A3LQ52; -.
DR   EnsemblFungi; ABN65153; ABN65153; PICST_88098.
DR   GeneID; 4837552; -.
DR   KEGG; pic:PICST_88098; -.
DR   eggNOG; ENOG502QUSW; Eukaryota.
DR   HOGENOM; CLU_019840_1_0_1; -.
DR   InParanoid; A3LQ52; -.
DR   OMA; HIYELNT; -.
DR   OrthoDB; 321092at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
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..62
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           63..629
FT                   /note="RNA-binding protein RMD9, mitochondrial"
FT                   /id="PRO_0000301788"
FT   REGION          28..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   629 AA;  73036 MW;  1224B6C1E68CC608 CRC64;
     MFRLVSSNAQ GSFRSSLLTK VRIPISVPAS SPLNTSTSNN TTTNNNNFGV NNSTNNTQFT
     RHQSSAAVDL SARKVYQDEF LRSHSSFTAP DHETKVKLNH FKELLVTGNQ KLRALNRQEA
     RAFYSVLQSL SHMLEDAKLR RSLNVDLLHQ YSLLLHSAIF SSRTNRLAEK RNRDKDEYNA
     TSYTDEVVLR GSVLNFAQLV EAGEFKYCFT DKVLQYLLYS MFQFKFNTEA LNLWENGVND
     AETGSVYLRP LVLATVLPRA FELKRFTYEE ILHIYELNTK KEQFPHHTLV TAMGKIAIHA
     GDYSRALDFL ERLLEKYDQK PTGLKLASLS DLHLSFIGDC KEIAIAKHFF DKVIEDELPY
     KVLLKVPYVT SLLDNAYQAG DSLEEAIYFW KNSVAYYMKT RQQLNSRYSL LNNKFFELFF
     QAYPELNEES FAMLRDLITF YAQTKPLDET FLNTIITHYS WKSKEVLDQL MQNYEIYEVE
     RTPVSHRICL KKTGQYADYT NEEILARWNE NLKCLDNSKY FYIPNADWSA LRDATIYSIV
     PDKRTDLYYS VLNTYKNYMQ DARACIKFVG NWTKRPAYLE SIARITLEKN FEPAVKVDVP
     LFRNLKENVN YADATRDLII TARNSKPRV