ID   EIF3M_ASPTN             Reviewed;         461 AA.
AC   Q0CPV5;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=ATEG_04279;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476599; EAU34726.1; -; Genomic_DNA.
DR   RefSeq; XP_001213457.1; XM_001213457.1.
DR   AlphaFoldDB; Q0CPV5; -.
DR   SMR; Q0CPV5; -.
DR   STRING; 341663.Q0CPV5; -.
DR   PRIDE; Q0CPV5; -.
DR   EnsemblFungi; EAU34726; EAU34726; ATEG_04279.
DR   GeneID; 4320491; -.
DR   VEuPathDB; FungiDB:ATEG_04279; -.
DR   eggNOG; KOG2753; Eukaryota.
DR   HOGENOM; CLU_035254_0_1_1; -.
DR   OMA; REDAQRC; -.
DR   OrthoDB; 679771at2759; -.
DR   Proteomes; UP000007963; 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; Reference proteome.
FT   CHAIN           1..461
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   M"
FT                   /id="PRO_0000366015"
FT   DOMAIN          205..376
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          42..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  50154 MW;  DFC873C08A65A65F CRC64;
     MPAPSTTLLI EGSFSELADE FAQYIDALRK TEPSLQAELS PLLEPLRQQE QSDAEPDRKQ
     RDEVLKKLVS AATVLNTAPE KEIISAYNLL VHLVHHASDP DMFLSRICSY LAKPITSSPQ
     FGPSLAISIL STIFNTLPAT DSSRYHVLLA IVAVIRQSAQ GVAFEALKPQ LTAQLPTWLA
     AWELDEDEAQ RLHLAIADAA QAAGDQELAQ THVVQALQTI PAADASKKEA RDLAVRALTS
     ALSHPAVFDF TPLTASDAVQ ALRTSDSTLF ELLEIFTADT LDAYEAFVAA TPLASISGGV
     LAPAADALQN KMRLLTLASL AASTPSRSLP YATIASALRV PAEDVEKWVI DTIRAGLVEG
     KLSQLRSEFL VHRATYRVFG EKQWAEVQGR LMVWRRSLEN VLGVVRSERE RFIRENLQAA
     QAAEEAAQGK SGDKKGDRRQ RRDQPQQSQP APEAATAVAA E