RMD9_CANGA
ID RMD9_CANGA Reviewed; 616 AA.
AC Q6FU02;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=RNA-binding protein RMD9, mitochondrial {ECO:0000250|UniProtKB:P53140};
DE Flags: Precursor;
GN Name=RMD9; OrderedLocusNames=CAGL0F07469g;
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: 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; CR380952; CAG59216.1; -; Genomic_DNA.
DR RefSeq; XP_446292.1; XM_446292.1.
DR AlphaFoldDB; Q6FU02; -.
DR SMR; Q6FU02; -.
DR STRING; 5478.XP_446292.1; -.
DR EnsemblFungi; CAG59216; CAG59216; CAGL0F07469g.
DR GeneID; 2887885; -.
DR KEGG; cgr:CAGL0F07469g; -.
DR CGD; CAL0131290; CAGL0F07469g.
DR VEuPathDB; FungiDB:CAGL0F07469g; -.
DR eggNOG; ENOG502QUSW; Eukaryota.
DR HOGENOM; CLU_019840_0_0_1; -.
DR InParanoid; Q6FU02; -.
DR OMA; DCVFQTL; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:EnsemblFungi.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:EnsemblFungi.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IEA:EnsemblFungi.
DR GO; GO:0009060; P:aerobic respiration; IEA:EnsemblFungi.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0006413; P:translational initiation; IEA:EnsemblFungi.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Sporulation; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..616
FT /note="RNA-binding protein RMD9, mitochondrial"
FT /id="PRO_0000301783"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 71001 MW; 48E9BFFD4F41F4FC CRC64;
MFRYLSRTST IYKGVIATSK TASTANVVAA QESRRNYANK RNNNRNGPAD ALDEKLNSIL
SGKTSSKRKP YGGRKSPVDE TSPWYAQLCA LDDCLTTTLK QSATPMRKLL SDRVNHPDMR
SNPTFWHSVS RAMTLYNELK QCPEMTDQRV TSLVHLLHNG LRTDRQLVSS LNKKPDYDSQ
SFHKEMVNFI YTSLNEISDD ILNNNVPINA NGLMHLFTSY QEMGFTDLVV QIWKKIETIA
EQNPQSNIGK ISKHPNVVGI VLPILYEKEI VNFSEAEKLF KECEQYHNRM FPNLYVGMIL
TSLKANENMK ALELFETLCT NSKGVHYGYI SETHIAFISQ CKDISVAESF LDKAVNNEMP
YRVEIQVSAV NSLMYNIWSE NQDFNKIKEI WQKMVTFYGE NNLRLAIFSS LNNEFFSYFF
EKYKENKTEG LEQLQKLITQ YNNLKGIDEP FLNIILAKCT VWKEPEVIKY IEKNFELFNV
PKSLITSRIL LKSLGSIDNI TKEQIVERWQ EIVLKADSLG SKYIANADWA ALRDATVKWA
QENKDNQESL DRIEWYLQIV NVYQKYCRDG SQRYRILKGC SKSFPILAEN LQRLDLVDTS
SIPVCEVKSL KEALQN