ID   EIF3M_EMENI             Reviewed;         459 AA.
AC   Q5B5C1; C8V418;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=AN4259;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000069; EAA58927.1; -; Genomic_DNA.
DR   EMBL; BN001302; CBF74373.1; -; Genomic_DNA.
DR   RefSeq; XP_661863.1; XM_656771.1.
DR   AlphaFoldDB; Q5B5C1; -.
DR   SMR; Q5B5C1; -.
DR   STRING; 162425.CADANIAP00004396; -.
DR   EnsemblFungi; CBF74373; CBF74373; ANIA_04259.
DR   EnsemblFungi; EAA58927; EAA58927; AN4259.2.
DR   GeneID; 2873678; -.
DR   KEGG; ani:AN4259.2; -.
DR   VEuPathDB; FungiDB:AN4259; -.
DR   eggNOG; KOG2753; Eukaryota.
DR   HOGENOM; CLU_035254_0_1_1; -.
DR   InParanoid; Q5B5C1; -.
DR   OMA; REDAQRC; -.
DR   OrthoDB; 679771at2759; -.
DR   Proteomes; UP000000560; Chromosome II.
DR   Proteomes; UP000005890; 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:0005852; C:eukaryotic translation initiation factor 3 complex; IBA:GO_Central.
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:0097308; P:cellular response to farnesol; IEP:AspGD.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
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..459
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   M"
FT                   /id="PRO_0000366019"
FT   DOMAIN          207..384
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          431..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   459 AA;  49846 MW;  73CD89F7E6BFC827 CRC64;
     MPAPSTTLLI EGSFSELAEE FAAYLDALNK PDDTTVQTEV APLLQPLREQ EQNDTQLDQS
     KRDEVLKKLV SAATVLNTAP EKEITPAYNL LIHLVQQASD PDMFLSRICS YLAKPIPSSP
     QFGASLSIAI LSTIFNTLAP TDSSRFHVLL AIVTVIRQSG SSAAFDALKP QLTAQLPNWR
     STWELDDEEA RRLHLAIADA AQAAGDLDWA QTHVVDALQT IPPAEASSPA ARDLAVRALT
     SALTHPAVFD FTPLTAADAV QALRSSDAPL FELLEIFTAD TLDAYEDFIS ATPVENILPD
     NALAPHAEAL QTKIRLLTLA SLAAAATTTT GPSARSLSYE TIASALRVPQ EEVEKWVIDT
     IRAGLVEGKL SQLRSEFLVH RATYRVFGEK QWAEVQGRLM VWRRSLENVL GVIRSERERF
     VREAAAAAAA AAAEGEKGDK NNKGPSERRR APQEIAAAE