ID G2YJD1_BOTF4 Unreviewed; 857 AA.
AC G2YJD1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 22-FEB-2023, entry version 48.
DE RecName: Full=Mitochondrial escape protein 2 {ECO:0000256|ARBA:ARBA00020222, ECO:0000256|RuleBase:RU367108};
GN ORFNames=BofuT4_P021240.1 {ECO:0000313|EMBL:CCD51818.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD51818.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; FQ790337; CCD51818.1; -; Genomic_DNA.
DR AlphaFoldDB; G2YJD1; -.
DR STRING; 999810.G2YJD1; -.
DR eggNOG; ENOG502QS0P; Eukaryota.
DR HOGENOM; CLU_007861_1_0_1; -.
DR InParanoid; G2YJD1; -.
DR Proteomes; UP000008177; Unplaced contigs.
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 InterPro; IPR018850; Mt_escape_2_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR039627; Yme2_C.
DR PANTHER; PTHR32198; MITOCHONDRIAL ESCAPE PROTEIN 2; 1.
DR PANTHER; PTHR32198:SF2; MITOCHONDRIAL ESCAPE PROTEIN 2; 1.
DR Pfam; PF10443; RNA12; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|RuleBase:RU367108};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU367108};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 206..298
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 96652 MW; 52D18A2EC1CF42FF CRC64;
MNRRILFNPT SVPALRTPRP PRLQTRAFGN VGNFARVGLK GLKYDRSKGM KGVRRESTQI
GENESGHITA GTNEGILFLD NIFPIKLGWL LRIPWYGRMD SGLPDILYRF NNKVFSKYDP
LSLVERAIPP SVPLKVTEIL PRLKEGGAFI KFSHDRSITT QEIERLISEY LKEKPIKPWF
NPFRQMRAKL VRGKPWLEDL YRFPSTRIRV EFVPSTPGGE VAELSQEVIY SLFRKYGKIA
EISSQPSDSK VLPKFAMLDF ANIRHSIMAR NCLHGLKVTE ELGGGKSGTI LRLSFEAKMQ
AHHIREWLTS HPRVVIPAVA AILATVTVAV FDPIRTFFIK AHIDHAFSLK DNKIYAWFAS
QAKDVFSFHV HKAEEASLSA IWDDRKQAIE DLQTWLMETA DTFIVVQGPR GSGKKELIID
QALKGRPNTL LIDCKPIQEA RGDSATIAAA AATVGYRPVF SWMNSFSSLI DLAAQGTIGV
KSGFSETLDS QLAKIWQNTA TALKQVALQN RKKGDKDDNL ADDDWLEAHP EQRPVVVIDN
FLHKNEDSSI VYDKISEWAA GLTTSNIAHV IFLTNDISYS KSLSKALPDR VFRQIALGDI
TPQVAKKFVI SHLENDPENP KDKTEKLSES QRREDLSELD ECIEVLGGRL TDLEFLARRL
KTGQTPKRAV AEIVEQSASE IMKMYLLSAE KGDRKWSVEQ AWYLVNSLAE NDTLRYNQVL
LSDTFKSSLT SSASNGENVL EALSAAELIT IKTFKGRPQS IKAGKPVYQA AFKMLSEDRV
LRSRLDLAVL TELTKIETKS IDKYENELVM LGTLPKQPYE VGPRIKYLLD KLAASQRKVE
AWEKEMGFLK KVLMVEY
//
