YME2_LODEL
ID YME2_LODEL Reviewed; 862 AA.
AC A5DSF0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Mitochondrial escape protein 2;
DE Flags: Precursor;
GN Name=YME2; ORFNames=LELG_00286;
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: Plays a role in maintaining the mitochondrial genome and in
CC controlling the mtDNA escape. Involved in the regulation of mtDNA
CC nucleotide structure and number. May have a dispensable role in early
CC maturation of pre-rRNA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the YME2 family. {ECO:0000305}.
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DR EMBL; CH981524; EDK42108.1; -; Genomic_DNA.
DR RefSeq; XP_001527766.1; XM_001527716.1.
DR AlphaFoldDB; A5DSF0; -.
DR STRING; 379508.A5DSF0; -.
DR EnsemblFungi; EDK42108; EDK42108; LELG_00286.
DR GeneID; 5234934; -.
DR KEGG; lel:LELG_00286; -.
DR VEuPathDB; FungiDB:LELG_00286; -.
DR eggNOG; ENOG502QS0P; Eukaryota.
DR HOGENOM; CLU_007861_1_0_1; -.
DR InParanoid; A5DSF0; -.
DR OMA; NPIKPWF; -.
DR OrthoDB; 213553at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd12433; RRM_Yme2p_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR018850; Mt_escape_2_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR039627; Yme2_C.
DR InterPro; IPR034260; Yme2_RRM.
DR PANTHER; PTHR32198; PTHR32198; 1.
DR Pfam; PF10443; RNA12; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 3: Inferred from homology;
KW Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW mRNA processing; Reference proteome; RNA-binding; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..862
FT /note="Mitochondrial escape protein 2"
FT /id="PRO_0000343124"
FT TOPO_DOM 37..282
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..862
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 176..267
FT /note="RRM"
FT COILED 820..847
FT /evidence="ECO:0000255"
SQ SEQUENCE 862 AA; 99075 MW; C01B6E7491C1F4DD CRC64;
MMRLKILRAS RINPALLRLR PPHLYSINKS QAFRFYATDI EDLKRQSDRT ESDNSASTTG
VIDKEANEVL LYYSFSNSRN FVKQYISRFL PSKFLGEQVE EKVKDVSYPL PQNSSITEVL
HLPRDSGAFV KFKYSPSLTA KEFIQDIRSN IAESNTKRYS NIFMKAIGFV WDRSTQVYTV
KGVPWIEDLK RFPSQKIGIT YEGNPLTEEE LYVLFRRYGL IDDIKVESTQ SFVLFDTVRA
AICAKHCITG MQLNGGKTTI HIQYVPVKKT NFIIEMISSH TKIALPIILA LLATFAVLIF
DPIREWFIQL KITRASHSFD EFKENKWFKI VYIPYKQLLN AVSSGYDYID TQLHEVTGIN
NVDECLDDNQ VLQEKNWESN MFWRERFEKA KQLKLWIMEN IDTFIIVKGP QGSGKEEFVV
DHTLMADAKL RKKVLLLECD ELSKARSENS LIASTASQLG YFPVFTWTNS ISQFIDLGLQ
GLTGQKSGLS ESKETQIKNM FSLATQAIRS LTDGDYNKYK TNIEKKNRRL KDDEKIEVLR
LEEFLAQHPE SKPIIVINKF ARKADVLSND FIFPLIADWA SGLIQNNIAH VVFTTADVGS
LQHLNDALPN QVFKNISLSD ASIASSKQYI CDALKMKDTA TLDDCIAPLG GRMLDLQAFI
RRIKSGEDPL QAIDEMVNQA AELITTFFLH EHKFSNDDSN WNPSQVWLIM KLLSKKDVID
YDSLIKLPLF KQSKETLDTL STLEKYDLVS LKREKGVLSK ILTGRPLFTA AFENIISDVR
IWKLYETQYL LNLVSLEVQK LTKFENELTT IYKINKLDGR IDYLSKKIDE SNQKIVDYEK
EIKDIAAYKG EPKQRHSFLG IF