YME2_ASHGO
ID YME2_ASHGO Reviewed; 806 AA.
AC Q751P7;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Mitochondrial escape protein 2;
DE Flags: Precursor;
GN Name=YME2; OrderedLocusNames=AGL358C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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}.
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DR EMBL; AE016820; AAS54133.1; -; Genomic_DNA.
DR RefSeq; NP_986309.1; NM_211371.1.
DR AlphaFoldDB; Q751P7; -.
DR STRING; 33169.AAS54133; -.
DR EnsemblFungi; AAS54133; AAS54133; AGOS_AGL358C.
DR GeneID; 4622602; -.
DR KEGG; ago:AGOS_AGL358C; -.
DR eggNOG; ENOG502QS0P; Eukaryota.
DR HOGENOM; CLU_007861_1_0_1; -.
DR InParanoid; Q751P7; -.
DR OMA; FQFFRPY; -.
DR Proteomes; UP000000591; Chromosome VII.
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; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; mRNA processing;
KW Reference proteome; RNA-binding; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..806
FT /note="Mitochondrial escape protein 2"
FT /id="PRO_0000343111"
FT TOPO_DOM 26..268
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..806
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 181..253
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ SEQUENCE 806 AA; 91664 MW; 58A3E8BFE6D5A176 CRC64;
MMFLEMQRAF MLHGRRAVTR SAVGVRYISE DIQQKDAQAG EKATATATGV IYKSDEETLM
YFDNVYPRAT SLWRPTQWYN ILLSNQSREA VREKIMRLAS PASNPVHGLE LRSTIPIKRD
GGVFATFRVP REYTRAQVNA LIQANTQQES SKSLLAAFTR AAAFPVKGVP WIEDLKRLPN
NVVRVEVEGP ALSEEELYSL FRRYGTILDI YPAGKNGYAT IRYRSFRGAI CAKNCVSGIE
INGSTLHVKF EPVVRAHAIR DFFVNHPRIA IPLLIALLSI CAVLIFDPIR EFSIEQKITR
MYTLSRDNFV VKSILRLTSY TVSSVKHLWG YDDDQPEKRQ LWQERVEKVN DLKMWLEENN
NTFVVVTGPR GSGKHELVMQ HTLHDRPNVL YLDCDTLIKS RTDSKFLRNA AHQIGYFPIF
PWLNSVTTLV DLAVQGLTGQ KSGLSESKET QFRNMLNTAM MSIRHIALSG YKATLHSGDD
VTTVKEEDYL QQHPERKPVI VIDRFSNKAE INGFVYKELA DWASMLVQMN IAHVIFLTES
VSPNQLLAEA LPNQVFKFLF LSDASKDSAR SYVLSQLYPS SPAYSEKMPA ADADANEEYR
KEIDRALEPI GGRMLDLQAF VRRVKSGEEP SEALEKMVEQ ASEQITQIFL SERSEPIKTA
QAWELIELLS QNDVVKYGDI VFRPLFKSSP EAGLLELEKN GLITISRNRG VLQDIRPAKP
LFKAAFSYLL QDKDLSIVLR TGYYLRLIAF ETGRIKKWEE ELRLLAKVSD QRICKSRLNY
LASKIDASSG VINSCEDKVK EMSKRI