ID   YME2_YEAS7              Reviewed;         850 AA.
AC   A6ZN18;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Mitochondrial escape protein 2;
DE   AltName: Full=Protein RNA12;
DE   Flags: Precursor;
GN   Name=YME2; Synonyms=PRP12, RNA12; ORFNames=SCY_4484;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000021; EDN64242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZN18; -.
DR   EnsemblFungi; EDN64242; EDN64242; SCY_4484.
DR   HOGENOM; CLU_007861_1_0_1; -.
DR   Proteomes; UP000007060; 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   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR018850; Mt_escape_2_C.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR039627; Yme2_C.
DR   InterPro; IPR034260; Yme2_RRM.
DR   PANTHER; PTHR32198; PTHR32198; 1.
DR   Pfam; PF10443; RNA12; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; mRNA processing;
KW   RNA-binding; Transit peptide; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..44
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..850
FT                   /note="Mitochondrial escape protein 2"
FT                   /id="PRO_0000343133"
FT   TOPO_DOM        45..287
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..850
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          198..272
FT                   /note="RRM"
FT   REGION          44..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  96659 MW;  DC6E2620AC3F6BAA CRC64;
     MLLVRTTSLN VSRMPVPCLA RGIGILKGKY RLANLMNAQP SVRHVSSEIQ QKDQQAGESN
     TATDTGVIHK SDEETLIYFD NVYARATSVW NPTLWYNLLL RNQSRDAVRE KIRNLASPPN
     NPIYGLELKS TIPVKRDGGV FATFVVPPKY TKAQVNSLIQ QNTARESSKN LLSYFTRVSA
     FPVKGSPWIE DLRRLPSTTI VIKFQGPALT EEEIYSLFRR YGTIIDIFPP TAANNNVAKV
     RYRSFRGAIS AKNCVSGIEI HNTVLHIQYE NIIRGHLVSN FFTNHTRIAI PVLFALLSIF
     AVLVFDPIRE FSIEQKITHK YSLSWDNKFW KQLKTLTSST MTSIKYYWGG PDDNHQRKHL
     WEERIEKVND LKMWLEENNN TFVVIRGPRG SGKHDLVMQH TLQNRANVLY LDCDKLIKSR
     TDPKFLKNAA SQLGYFPIFP WIDSVTGVLD LTVQGLTGQK TGLSETKESQ FRNMLTTSLM
     SIRRIALKNY KAFVSTGDGT VNVKEEDYLQ QHPEAKPVIV IDRFEGKSEI NGFVYKELSD
     WAAMLVQMNI AHVIFLTETV ASNQRLSESL PNQVFKNLIL SDASKENSRN YVLSQLEDYL
     YYNKKSKGEN VKEPESEKEI AENNDSDSEA DTSVKEAEVI LNEKELQEID ASLEPLGGRM
     LDLQAFVRRV KSGEEPSEAL DKMIEQASEQ ITQMFLSDKI DSNKSAQAWE LIELLSANPV
     IPFREIVNKP LFKAAPETGI MELENNGLIT VSRDRGVLQE IRPAKPLYRA AFTYLINDPE
     LAKVLKTRYL LKVVGFETGR IKKWEEELKP LGKVPDQKLF KTRLDYLSGK INASNAVITK
     CEEEIKNLSK