ID   YME2_CANAL              Reviewed;         867 AA.
AC   Q5A061; A0A1D8PSM3; Q5A009; Q5A037; Q5A089;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Mitochondrial escape protein 2;
DE   Flags: Precursor;
GN   Name=PRP13; Synonyms=PRP12, PRP121, PRP122, YME2;
GN   OrderedLocusNames=CAALFM_CR03810WA;
GN   ORFNames=CaO19.11829, CaO19.11857, CaO19.4351, CaO19.4379;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP017630; AOW31119.1; -; Genomic_DNA.
DR   RefSeq; XP_715128.2; XM_710035.2.
DR   AlphaFoldDB; Q5A061; -.
DR   STRING; 237561.Q5A061; -.
DR   GeneID; 3643194; -.
DR   KEGG; cal:CAALFM_CR03810WA; -.
DR   CGD; CAL0000185129; PRP13.
DR   VEuPathDB; FungiDB:CR_03810W_A; -.
DR   eggNOG; ENOG502QS0P; Eukaryota.
DR   HOGENOM; CLU_007861_1_0_1; -.
DR   InParanoid; Q5A061; -.
DR   OrthoDB; 213553at2759; -.
DR   PRO; PR:Q5A061; -.
DR   Proteomes; UP000000559; Chromosome R.
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   InterPro; IPR018850; Mt_escape_2_C.
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..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..867
FT                   /note="Mitochondrial escape protein 2"
FT                   /id="PRO_0000343116"
FT   TOPO_DOM        26..279
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301..867
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          179..264
FT                   /note="RRM"
FT   COILED          795..852
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   867 AA;  99327 MW;  06E524685F470F4A CRC64;
     MIIRTLRSQL RLPKPVYISP PCRYYSTDLE KLKKESDTTE SDNSASATGV IDKTHNEVLL
     YYDHIYPFTT SRNVVKQYLS RFSLPWSTAY DDEKLKQKVW DLSSPLETTA KITEFVPLRR
     DCGAFVKFKY PPEVPATKFI EEIRENVEKN EQERVNSNIL TKLYHQIWRN VPKVYSVKGT
     PWIEDLRRFP SPKLSVKFEG DPLTEEELYV LFRRYGLINE IEPGATEAFI YFHSTRAAIS
     AKHCITGMVL NGGKTTLHIQ FVAIKRSNFL VSLISNHTKI AIPVLIALLA TFAVLIFDPI
     REWFIEYKIL HNRKSFDQFK ESRWFKYLYI PYRTITGWVY SSYDYIDSQI QEVTGSSCSE
     EDDSSNGSNI VDGQSVRDLK NESNMFWIER YEKSKQLQLW IMENANTFII VKGPQGSGKE
     EFVLEHSLGS DERLNKKVLV LECDQLGKAR SDNNLINTTA SQLGYFPVFT WTNTVSRFVD
     LGVQGLTGQK SGLSESKETQ IKNMFSLATQ AIRKITTNEY NKYVKSVERR NKRLKDDEKI
     EVLKEEQFLQ QHPEAKPIIV LNKYSRRADV SSNDFIPPLV ADWASGLVQN NTAHVIFLTA
     DVGSLQLLND ALPNQVFKDI SLSDASMSSS RQYVCDVLKV KDTSTLDECL EPLGGRMLDL
     QSFIRRIKSG ESPQQAINEM ISQAAELINT FFLNSHHKFG AGDSNWDPSQ VWLIMKLLSE
     CDTINYSELV KSPLFKVSKE TLEILTTLEK YDLISLKRDK GVLDKISTGR PLFKAAFANI
     ISDLRIWKLY ETEYIGRLIS LEAAKIQKLE EELEKIYKIG KVDGRIDYVS QKIEASNKKI
     LDLEKQAADV ASYTGKPDGK SFLGIKF