RM02_DEBHA
ID RM02_DEBHA Reviewed; 394 AA.
AC Q6BIE4;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=54S ribosomal protein L2, mitochondrial;
DE Flags: Precursor;
GN Name=MRPL2; OrderedLocusNames=DEHA2G11176g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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: Component of the large subunit of mitochondrial ribosome.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family.
CC {ECO:0000305}.
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DR EMBL; CR382139; CAG90511.1; -; Genomic_DNA.
DR RefSeq; XP_462027.1; XM_462027.1.
DR AlphaFoldDB; Q6BIE4; -.
DR SMR; Q6BIE4; -.
DR STRING; 4959.XP_462027.1; -.
DR EnsemblFungi; CAG90511; CAG90511; DEHA2G11176g.
DR GeneID; 2904935; -.
DR KEGG; dha:DEHA2G11176g; -.
DR VEuPathDB; FungiDB:DEHA2G11176g; -.
DR eggNOG; KOG4600; Eukaryota.
DR HOGENOM; CLU_063752_0_0_1; -.
DR InParanoid; Q6BIE4; -.
DR OMA; FYLDPFH; -.
DR OrthoDB; 1177118at2759; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR InterPro; IPR001684; Ribosomal_L27.
DR InterPro; IPR041244; Ribosomal_L27_C.
DR InterPro; IPR018261; Ribosomal_L27_CS.
DR PANTHER; PTHR15893; PTHR15893; 1.
DR Pfam; PF01016; Ribosomal_L27; 1.
DR Pfam; PF18471; Ribosomal_L27_C; 1.
DR PRINTS; PR00063; RIBOSOMALL27.
DR TIGRFAMs; TIGR00062; L27; 1.
DR PROSITE; PS00831; RIBOSOMAL_L27; 1.
PE 3: Inferred from homology;
KW Mitochondrion; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 35..394
FT /note="54S ribosomal protein L2, mitochondrial"
FT /id="PRO_0000030499"
FT REGION 36..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 45231 MW; CD4C319A90FA5069 CRC64;
MSFIKQVGKL IRPNDYSSSI FQTSFLNNVI QVRTATKRAA GSKTNKNDSA GRRLGPKAYE
GHFVKPGQII MRQRGTKIHP GENVDIGKDH TIFAIEPGYV RFYYDPFHPL RKYVGIALRK
DLNLPTPHFS PRVRRFGYEK ITDPAEAEKE ENHMSRKEFL QQPELEKTRQ EQQNQEEQRA
SAFRNALSSQ FNLDLSEADF QLALNRLLNI SQLTNVGQTL EDAEVQSTYN YVFDLKLSCK
RGEMTSEEFS NLKMHYIQFA ENFDKKVTID AQGNPCTYVT PEAKKENQNE ILSKLENEFS
NRVISEKDKE TIFDLIMTPG IYNLSQQSYL KDRFLPSVLP TTVKETVVED VDPKKPPKGV
IVTRIFDEET KQIKVIGRTK EAYIGQTDLD KSLA