ID   YME2_NEUCR              Reviewed;         867 AA.
AC   Q873L8;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Mitochondrial escape protein 2;
DE   AltName: Full=mRNA-splicing protein 45;
DE   Flags: Precursor;
GN   Name=msp-45; Synonyms=yme2; ORFNames=B18E6.070, NCU09598;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD70287.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; BX284745; CAD70287.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002237; EAA33940.2; -; Genomic_DNA.
DR   RefSeq; XP_963176.2; XM_958083.3.
DR   AlphaFoldDB; Q873L8; -.
DR   STRING; 5141.EFNCRP00000009426; -.
DR   EnsemblFungi; EAA33940; EAA33940; NCU09598.
DR   GeneID; 3879324; -.
DR   KEGG; ncr:NCU09598; -.
DR   VEuPathDB; FungiDB:NCU09598; -.
DR   HOGENOM; CLU_007861_0_0_1; -.
DR   InParanoid; Q873L8; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IBA:GO_Central.
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..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..867
FT                   /note="Mitochondrial escape protein 2"
FT                   /id="PRO_0000343127"
FT   TOPO_DOM        42..308
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..867
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          203..293
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          44..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          797..857
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        46..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..636
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   867 AA;  97179 MW;  861FBB772A4218C2 CRC64;
     MISAHILSRQ ATRPGHRGPR FTTHSTALLV QRSLGQGLPL AHRRTTRAWE STSSSTASTG
     SHKESGHIET APHESLLFFN NLFPLKLSSI LIWRPWTSED LLQRFEQSSY SFIDPIRLVK
     RAINTHDQVP IEVTQIIPRL KDGGAFVKFT HPSDMSAAVV ESKLSELLQN NPIKPWFNPF
     GRVKAGLVEG VPWLEDLYRL PRSRIRVEFV AAKDDASPAE LSQETLYSIF RKFGKITEIT
     SQPTDSKVLP RFAYIDFVLV RDAIMARNCM HGFVLREQGS KNATKLRLSY EQRVKAHHIW
     AWFTSHPRIV IPLVAALIAA FTVAVFDPIR EFFVKAHVQK YFEFTNSRLY KWFKSQTSDI
     LAFRRRKTED AGLNALFTHR KDLIDSIQTG LLESVDTFTV VHGPRGSGKK ELILDQVLKE
     RSNVLHIDCK PVVEARGEAG TIGRLAFEVG YRPVFSWSNN ISSLVDLAVQ STTGVKANFS
     ENLESQVVKI LQTTASALKQ VGLSERKKED KDADLSEDAY LEAHPERRPV IVIDHFLHKS
     EEKGVIYDRI ADWAAALVQS NIAHVIFLTD DASYSKPLQR SLPDRVFRSV TLGDLSPDVA
     KKFVISQLQT DTKFAHDGQQ KDSESGDQDN DNKNQKKDSN TPAPLDPTLL KELDTCITAL
     GGRLTDLQVL ARRLKIGQSP RKAVQEIIDS TASDILRMFL LSKSSTSDRK YTTEQAWYLI
     SHLAASPSSS IPYNSVLLSN TFASSPETAL EALANAELIT VKSQNGMPSE IKAGKPVYQA
     AFQKLASDEK VKARMDLLVL TELAKMETQK IEKVEQELVM LQGLMARRPG DVSERVEYLL
     EKMKGGQARL KGLEKEMGVV KGQMVKG