ID   EIF3M_ASPFC             Reviewed;         468 AA.
AC   B0YCA6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=AFUB_089510;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499601; EDP48237.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0YCA6; -.
DR   SMR; B0YCA6; -.
DR   EnsemblFungi; EDP48237; EDP48237; AFUB_089510.
DR   VEuPathDB; FungiDB:AFUB_089510; -.
DR   HOGENOM; CLU_035254_0_1_1; -.
DR   PhylomeDB; B0YCA6; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
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; IPR045237; COPS7/eIF3m.
DR   InterPro; IPR027528; eIF3m.
DR   InterPro; IPR040750; eIF3m_C_helix.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR15350; PTHR15350; 1.
DR   Pfam; PF18005; eIF3m_C_helix; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis.
FT   CHAIN           1..468
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   M"
FT                   /id="PRO_0000366012"
FT   DOMAIN          206..377
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          40..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  51113 MW;  CAFA2874DECFB934 CRC64;
     MPAPTTTLLI EGSFTELADE FAQYIDALRK NEGASLQSEV APLIEPLRQQ EQSEEEPDRK
     QRDEVLKKLV GAAAVLNAAP EREIISAYNL LVHLVHQASN PDIFLSRICT YLAKPITTSP
     QFGPTLAISI LTTIFNTLAP TDSSRFHVLL AIVAVIRQSG SSYAFEALKP QLAAQLPTWL
     SAWELDDEDA QKLHLAIADA AQASGDLELA QTHVVQALQT IPANESSSKE ARDLAVRALT
     SALKSPAVFD FTSLTAADAI QALRSSDSTL FELLEIFTAD TLDAYEDFIA ATPLETISGG
     VLVDGAEALQ TKMRLLTLAS LAASTPSRSL PYTTIASALR VPVEDVEKWV IDTIRAGLVE
     GKLSQLRSEF LVHRATYRVF GEKQWAEVQG RLMVWRRSLE SVLGVLRTER ERYIRESMQA
     AAEEVGQGKS GDKGAKGGDR RRNPQQQQQS QPSQPQQARE VELVGGAE