ID A0A2T4BNQ0_9HYPO Unreviewed; 835 AA.
AC A0A2T4BNQ0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 02-APR-2025, entry version 20.
DE RecName: Full=Mitochondrial escape protein 2 {ECO:0000256|ARBA:ARBA00020222, ECO:0000256|RuleBase:RU367108};
GN ORFNames=BBK36DRAFT_1165434 {ECO:0000313|EMBL:PTB70948.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB70948.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) 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: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU367108}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004434,
CC ECO:0000256|RuleBase:RU367108}.
CC -!- SIMILARITY: Belongs to the YME2 family. {ECO:0000256|ARBA:ARBA00010320,
CC ECO:0000256|RuleBase:RU367108}.
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DR EMBL; KZ680207; PTB70948.1; -; Genomic_DNA.
DR RefSeq; XP_024754268.1; XM_024894775.1.
DR AlphaFoldDB; A0A2T4BNQ0; -.
DR GeneID; 36602893; -.
DR OrthoDB; 10267654at2759; -.
DR Proteomes; UP000241546; Unassembled WGS sequence.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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 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 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, ECO:0000256|RuleBase:RU367108};
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:UP000241546};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176,
KW ECO:0000256|RuleBase:RU367108};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367108};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367108}.
FT TRANSMEM 288..312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367108"
FT DOMAIN 180..272
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 20..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 93248 MW; AD7A55961E892E6F CRC64;
MRYRAGQRIW ETTSAIPLSD GNLTGKKQEL SPSEEQESGR FDVKPNESIL FFDNLFPLKL
TPVLSLLSRR TETDQQLTDL LQRFNSSSLG IMDPIQLVKR AIPDNLPIKV TEIMPRLKDG
GAFVKFEYDP SLSASEIEAK LLKKLREEPV KPWFNPFGRI RARLVRGVPW LEDLHRYPST
LVMVEFVPPE PGAAAAELPE EVLYSLFRKY GKIADIIPQP ADSKITPRYA QIGFPVLRDA
IMARNCLHGF VLGEAQGGGK NGTKLRLSYV KKEKGHSIWN WITSHPRIVI PIVAALIAGV
SVMIFDPIRL FFIKVHVQHS LRYTDWRIYK WFKSQTGSFS FHKKQEHIEG LGTIWKHRKD
LIEQLQSWLD GSSDTFIVVT GPRGSGKAEM VMSQALSGRK NVLLIDCKPI TEANGEAGTI
KRLATAVGYR PVFSWANSIS SMVDLAVQGT TGVKSGFSET LESQLNKILH TTATALKTVA
LSERSKADKD INLSEDAYLE AHPERRPVIV VDNFLHKSED SSLVYDMIAD WAATIVQNNV
AHVVFLTSDS AYSKSLTKAM PDRVFRTLSL GDLDADVAKN FVITRLEEDW KREAQEEAEQ
SDEEKKAIPR PNLAGLDEGI KVLGGRLTDL EFLARRLRAG QTPREAVEEI VTEDATDIVK
MYLLGRTADA DRKWSTEQAW HLIKSLSENP TLRYHQVLLS PTFASSLSSN ATNGEAAIES
LAGSELITVT THQGRPQTIT AGKPLHQAAF GVLVKDRVLR AKMDLAVLNE MAKVEAKNID
AVEKELQLLG GLPRHTGESA GRVMYLLGKL DAGQRKIAQL EREMGGLKRI MNEEY
//