ID   EIF3M_MAGO7             Reviewed;         432 AA.
AC   A4RK68; G4MTX3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit M {ECO:0000255|HAMAP-Rule:MF_03012};
DE            Short=eIF3m {ECO:0000255|HAMAP-Rule:MF_03012};
GN   ORFNames=MGG_01595;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis of a
CC       specialized repertoire of mRNAs and, together with other initiation
CC       factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC       ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000255|HAMAP-Rule:MF_03012}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03012}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03012}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit M family. {ECO:0000255|HAMAP-
CC       Rule:MF_03012}.
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DR   EMBL; CM001232; EHA54767.1; -; Genomic_DNA.
DR   RefSeq; XP_003714574.1; XM_003714526.1.
DR   AlphaFoldDB; A4RK68; -.
DR   SMR; A4RK68; -.
DR   STRING; 318829.MGG_01595T0; -.
DR   EnsemblFungi; MGG_01595T0; MGG_01595T0; MGG_01595.
DR   GeneID; 2679451; -.
DR   KEGG; mgr:MGG_01595; -.
DR   VEuPathDB; FungiDB:MGG_01595; -.
DR   eggNOG; KOG2753; Eukaryota.
DR   HOGENOM; CLU_035254_0_0_1; -.
DR   InParanoid; A4RK68; -.
DR   OMA; REDAQRC; -.
DR   OrthoDB; 679771at2759; -.
DR   Proteomes; UP000009058; Chromosome 2.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03012; eIF3m; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR045237; COPS7/eIF3m.
DR   InterPro; IPR027528; eIF3m.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR15350; PTHR15350; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..432
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   M"
FT                   /id="PRO_0000366020"
FT   DOMAIN          184..356
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          392..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  49620 MW;  E527A65FC9446D51 CRC64;
     MTASYQPQLV FVDGSFAELA QDMASVLQIS DEIQPLLDSE KESEALTKIV SESKKLNAIP
     EKEFTGAYNL LVHLVLQSKE PKKHLPTICQ NLTRPVTSSP QHGAQLALFE LTSIFNLLKP
     NDPVRFNVFI QIIRFYKIHS IPISDHLKSA LKQLPRWLQS WELDEEDQRK MYSEVIEVMT
     AAGEEEEAYQ HILKALRTFD SEDAEDYTSE EAQQLALRAL RSAISSPTRL SFEDIRALPA
     VHALSESHPV HYQLLQIFGE QDLDDYDDFR EEHEGFIEKE NLDNEVLYRK MRLLTFASLA
     AASMQTREIS YNSITKALQI PSEDVEMWAI DVIRAGLVEG KLSQKKKVFL IHSVRYRVFG
     EKQWRQLASS LEKTKKTVST LLQTLRREEA NAQQEAERKL VEASTQHNND RGNQRRGGNR
     GQQHRERNDN DD