ID K1XG76_MARBU Unreviewed; 850 AA.
AC K1XG76;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Mitochondrial escape protein 2 {ECO:0000256|ARBA:ARBA00020222, ECO:0000256|RuleBase:RU367108};
GN ORFNames=MBM_01765 {ECO:0000313|EMBL:EKD19813.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD19813.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD19813.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD19813.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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}.
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DR EMBL; JH921430; EKD19813.1; -; Genomic_DNA.
DR RefSeq; XP_007289654.1; XM_007289592.1.
DR AlphaFoldDB; K1XG76; -.
DR GeneID; 18757700; -.
DR KEGG; mbe:MBM_01765; -.
DR eggNOG; ENOG502QS0P; Eukaryota.
DR HOGENOM; CLU_007861_1_0_1; -.
DR InParanoid; K1XG76; -.
DR OMA; FQFFRPY; -.
DR OrthoDB; 1384689at2759; -.
DR Proteomes; UP000006753; 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 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 Pfam; PF00076; RRM_1; 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:UP000006753};
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 199..291
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
SQ SEQUENCE 850 AA; 95576 MW; E2561B9C58A48FC6 CRC64;
MQSSRRIYFN PTSIPGLRSQ KPVRRDFYNA GFTPRTGLRK DAKFTGGVRR ESTDTGEDQT
GHIAAGSNEG ILFFDNIFPL KLNWALRLPW KSEQSLPELL TRFNTSSLGT FEPVALVKRA
IPSSVPMKVT EILPRLKDGG AFVKFSYPDG ITAKEVEGLV RQYLREKPVK PWFNPFRRIR
ANLVVGKPWL EDLYRFPSSR MKVEFVPTSP GGEAAELSQE TLYSLFRKYG KLAEISPQPS
DSKILPKYAY LDFARLRHAI MARNCMHGLK VLETEGGGAA GTQLRLSFEQ RRKAHWIWDW
LMSHPRIVIP AFAALVATIT VAIFDPIRTF FIKAHIEHSF DLKDSRVYQW FKSQATDIFT
FRSHRAEEAS LDVLWGDRKQ IIDQLQTWLM ETADTFIVVQ GPRGSGKKEL ILDQALKGRK
NTVLIDCKPI QEARGDSATI SAAAASVGYR PVFSWMNSLS SLVDLAAQGT IGVKSGFSET
LDAQLSKIWQ NTAIALKQVA LQNRHKDDKD ATLADDDWLE AHPECRPVVV IDNFLHKNEE
SSVVYDKISE WAAGLTTANI AHVIFLTNDI SYSKSLSKAL PDRVFRQLAL GDITPEVAKR
FVITHLDSDQ NDPSGTSVKL TPRQRYHDLD ELDGAIAAVG GRLTDLEFLA RRLKTGQTPK
RAIAEMIEQS ASEIMKMYLL TVDKAERKWS PEQAWYLIKS LAENDSLRYN EVLLSNTFTS
SLNAFASNGE SVLEALSAAE LITIKSYKGR PQTVKAGKPI YEAAFKILAE DRVLKSRLDL
AILTELTKIE TKSLDKYETE LALIGTLPKQ PREVGPRVQY LLGKLAASQV KIEAWEKEMA
GLKKVLMDEY
//
