ID   YME2_ASPNC              Reviewed;         832 AA.
AC   A2QPL8;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Mitochondrial escape protein 2;
DE   Flags: Precursor;
GN   Name=yme2; ORFNames=An07g09890;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(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; AM270154; CAK39755.1; -; Genomic_DNA.
DR   RefSeq; XP_001392064.1; XM_001392027.1.
DR   AlphaFoldDB; A2QPL8; -.
DR   PaxDb; A2QPL8; -.
DR   PRIDE; A2QPL8; -.
DR   EnsemblFungi; CAK39755; CAK39755; An07g09890.
DR   GeneID; 4982258; -.
DR   KEGG; ang:ANI_1_2178064; -.
DR   VEuPathDB; FungiDB:An07g09890; -.
DR   HOGENOM; CLU_007861_1_0_1; -.
DR   Proteomes; UP000006706; Chromosome 4L.
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   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 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..40
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..832
FT                   /note="Mitochondrial escape protein 2"
FT                   /id="PRO_0000343114"
FT   TOPO_DOM        41..294
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        316..832
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          187..279
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   COILED          766..831
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   832 AA;  94310 MW;  554BCB2A6A8AED9C CRC64;
     MMRIPYRAVV PRATLLHARF SRPPAVPSLT KAFIVSRRTS SHASFIETGH IDVKDDEGLV
     FVNNIFPSKL QWLLQGPLSG NKTYEEALKR INRPHLAASD PLHIIRRVFP QSLNVDIREV
     IPRFREGGAF VKYVRKDGVR DNDIVTAVQH HLEHNPIRPW FNPFQQVKVA HVHGRPWIED
     LYRIPSQRLR VEFLPGSVDG AATELTTETL YSFFRRYGKL RDIERQPTDS KIAPRYAFVS
     FTRQKYAVMA KNCMHGFTIP EEEGGGKSGT RIKIKYERKI KFSVIKDWIL NHPRIVIPAI
     AALIAAITVT IFDPIRTFFI EMKIKATLQT EENSVLQWIR NQANKANIIY FGRQRTDPRR
     LTAIWEDRQG DIKQLQSWLM ENAETFIVIH GPRGTGKREL VLDRALENYK YKVVIDCKQI
     QDAKGDTAKI ARAASQVGYR PVFSWMNSMS SFIDLAAQGM IGTKAGFSET LDAQLSKIWQ
     NTATALKRVA LSNRKKDDKE AHLSDEEYLE AHPEQRPVVV IDNFLHNATE SSVVYDKITE
     WAAGLTTGNI AHVVFLTTDV SFSKPLSKAL PNSVFRTISL GDCSLDVGRK FVLSHLEHGA
     KDGANSGQNM EEVGDLGTLD SCIEVLGGRV TDLEFMARRI ESGETPRAAV NRIIEQSASE
     ILKMFVFDPD IESKQWSHEQ AWHLIKTLAH SQDGTLPYNQ VLLSDLFKEN GETTLRALEQ
     AELIAISSVN GCPDAVKPGK PVYRAVFKRL TENKTLSSRL DLDIVKQLLS SENKSIGKYE
     QELQVLGSLP KQPRELSARI QWLLQKVASS QNKISQYEHE SAILQKVLRR EH