YME2_NEOFI
ID YME2_NEOFI Reviewed; 869 AA.
AC A1D3P4;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Mitochondrial escape protein 2;
DE Flags: Precursor;
GN Name=yme2; ORFNames=NFIA_017380;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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=EAW23037.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DS027688; EAW23037.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_001264934.1; XM_001264933.1.
DR AlphaFoldDB; A1D3P4; -.
DR STRING; 36630.CADNFIAP00002147; -.
DR EnsemblFungi; EAW23037; EAW23037; NFIA_017380.
DR GeneID; 4591789; -.
DR KEGG; nfi:NFIA_017380; -.
DR eggNOG; ENOG502QS0P; Eukaryota.
DR OrthoDB; 103839at2759; -.
DR Proteomes; UP000006702; 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 InterPro; IPR018850; Mt_escape_2_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
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 Membrane; Mitochondrion; Mitochondrion inner membrane; mRNA processing;
KW Reference proteome; RNA-binding; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..869
FT /note="Mitochondrial escape protein 2"
FT /id="PRO_0000343126"
FT TOPO_DOM ?..334
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..869
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 227..319
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ SEQUENCE 869 AA; 98686 MW; 4FAD3883C88F4914 CRC64;
MIDVISRYQA SPLIESTLGY QSITIIFGNA HLQSSKKNVI LAAMMRTRIP GLVPRICQTP
LPWKPPTQLT RVRYARWSTS HAVSWFETGH IDLKENEGLL FINNIFPSKL QWLLRGPLGG
MRSYEEAVKR IDRPQLAASD TFQIIQRVVP KNLNIQVKEV VPRFREGGAF VKYTRPSNVN
DADIEASIKE NLKEHPIRPW FNPFQEVQVC RVIGRPWIED LYRLPSPRLK VAFHPVSPEA
SAADLNTETL YTLFRPYGKI RDIEKQPSDS KVTPRYAFVE FSRPKYAGMA KNCMHGFTVP
EQEGGGKSGT RLKIKYERKI KLSMIKDWLL SHPRIVIPVL AALLAAITVT IFDPMRTFFI
KLKIKSTLQT EENGVMQWIR KQVNKANIIY FGRKGADPRG LTAIWEDRQE DITRLQSWLM
ENVETFIVVH GPRGSGKREL VLDRALVDYK YKIVIDCKQI QDARGDSAKI ARAASQVGYR
PVFSWMNSIS SFIDLAAQGM IGTKAGFSET LDAQLSNIWQ NTATALKKVT LEHRKKNHKD
SHLTDEEYLE AHPELRPVVV IDNYLHNASE SSVVYDKITE WAAGLTAGNI AHVIFLTTDV
SYAKPLSKAL PNSVFRTITL GDCSLEVGRK FVVNHLAYES KDGKTQPRRA EELEDLDACI
ETLGGRVTDL EFMAHRIEAG ETPRGAVNRI IEQSASEILK MFLLTPETIE QSWTHEQAWY
LIKRLAESKD GALSYNEIVL SELFKENGEI TLRALEHAEL ISIAAVNGCP QTIRPGKPVL
RAAFKKVTEN KALSSRMDLA IITQKINKEN KSIGKYEEEL SLLGSLPRQP RELTDRIQWV
LNKVYSSQNK IAKYEKESAY LQKILRSEH