ID J7S7L2_KAZNA Unreviewed; 813 AA.
AC J7S7L2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Mitochondrial escape protein 2 {ECO:0000256|ARBA:ARBA00020222, ECO:0000256|RuleBase:RU367108};
GN Name=KNAG0E01300 {ECO:0000313|EMBL:CCK70396.1};
GN OrderedLocusNames=KNAG_0E01300 {ECO:0000313|EMBL:CCK70396.1};
OS Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS naganishii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK70396.1, ECO:0000313|Proteomes:UP000006310};
RN [1] {ECO:0000313|EMBL:CCK70396.1, ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2] {ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Kazachstania naganishii.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025276,
CC ECO:0000256|RuleBase:RU367108}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434,
CC ECO:0000256|RuleBase:RU367108}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU367108}.
CC -!- SIMILARITY: Belongs to the YME2 family. {ECO:0000256|ARBA:ARBA00010320,
CC ECO:0000256|RuleBase:RU367108}.
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; HE978318; CCK70396.1; -; Genomic_DNA.
DR AlphaFoldDB; J7S7L2; -.
DR STRING; 1071383.J7S7L2; -.
DR eggNOG; ENOG502QS0P; Eukaryota.
DR HOGENOM; CLU_007861_1_0_1; -.
DR OMA; FQFFRPY; -.
DR OrthoDB; 1384689at2759; -.
DR Proteomes; UP000006310; Chromosome 5.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd12433; RRM_Yme2p_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; MITOCHONDRIAL ESCAPE PROTEIN 2; 1.
DR PANTHER; PTHR32198:SF2; MITOCHONDRIAL ESCAPE PROTEIN 2; 1.
DR Pfam; PF10443; RNA12; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU367108};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|RuleBase:RU367108};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU367108};
KW Reference proteome {ECO:0000313|Proteomes:UP000006310};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU367108};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 186..259
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
SQ SEQUENCE 813 AA; 92905 MW; B710C2690FD035E5 CRC64;
MFLNRLSGLR TGPLRFRSLG SPRLSLCRAN RFVSSEIQAK DEQVGESNTA TNTGVILKSE
RETLVYFDNV YPRELSVWNP LLWYNSLFVD QSREAIRSRL VRLASPRSAP IPGLELQSSI
PVKRDGGVFA TFLVPRQYTL AEVNSMISQN TANESSKSPF SFFTTIAAFP VKGSPWIEDL
RRIPNKTIIV KFQGPSLTEE EMYLLFRRYG TIIDIYPPKD TENFAKVRYR SYRGAICAKN
CVSGMEINNT VVHIQYEKVK KTPFVTSFFV NHTRIAVPVF FALLSIVAVL IFDPIREFSI
EQKITHRYSF STENYWVKKL KNFTNSTVTQ FKSYWTGHGA EHPMIHLWGE RVERVEDLKM
WLEENSNTFV VIRGPRGSGK RELVMEHTLR ERDNVLYFDC DRIVKSRTDS KFLKSVANEL
GYFPIFPWIN SFTTIIDLMV QGLTGQKTGL SESKEAQFRN MLTTSLLAVR RIALKGYKQN
VTENNEVVNI KEEDYLQQHP EAKPVIVIDR FAGKSDMNAF VYKELADWAA MLVQMNIAHV
IFLTETIASD EILSESYPNQ VFKTLILSDA TKLSAKKYVL SQLEDHHEIQ DKSKDEKTVP
DLNPSVIEEI DEALDPLGGR MLDLQAFVRR VKSGEDPLKA LEKMVEQASA QITQIFLSDK
VDGVQSAQAW ELIEMLSKTP VISFKDIVFK PLFKAAPELG VIQLENNGLV SVSRNRGVLE
EIRPAKPLFR AAFSYLVQDD ELHVVLKTRY LLRVVAFETG RIKKWEEELK PLGKIADQKL
FKSRLDYLSG KIKASSQVID RCESDIKDLS TKK
//
