EIF3M_ASPOR
ID EIF3M_ASPOR Reviewed; 466 AA.
AC Q2UDZ9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=AO090026000816;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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; AP007159; BAE60216.1; -; Genomic_DNA.
DR RefSeq; XP_001822218.1; XM_001822166.2.
DR AlphaFoldDB; Q2UDZ9; -.
DR SMR; Q2UDZ9; -.
DR STRING; 510516.Q2UDZ9; -.
DR EnsemblFungi; BAE60216; BAE60216; AO090026000816.
DR GeneID; 5994246; -.
DR KEGG; aor:AO090026000816; -.
DR VEuPathDB; FungiDB:AO090026000816; -.
DR HOGENOM; CLU_035254_0_1_1; -.
DR OMA; REDAQRC; -.
DR Proteomes; UP000006564; Chromosome 3.
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..466
FT /note="Eukaryotic translation initiation factor 3 subunit
FT M"
FT /id="PRO_0000366014"
FT DOMAIN 211..378
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 40..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 50769 MW; 01FD4DB13EFF3354 CRC64;
MPAPTTTLLI EGSFSELADE FAQYLDALRK SEGTTTIQAE ISPLLEPLRQ QEQSDAEPDR
KQRDEVLKKL VSAASVLNNA PEKEIISAYN LLVHLIHYAS DPDMFLSRIC SYLAKPITSS
AQFGPSLAIS ILSTIFNTLA PTDSSRFHVF LGIVAVIRQS GSTVAFEALK PQLTAQLPTW
LSSWELDEEE AQRLHLAVAD AAQAAGDPEL AQTHILQALQ TIPAAQASSK EARDLAIRAL
TSALTHPAVF DFTPLTASDA VQALRSSDST LFELLEIFTA DTLDAYEAFV TATPLAGISG
GVLADAGEAL QNKMRLLTLA SLAASTPSRS LPYATIAASL RVPAEDVEKW VIDTIRAGLV
EGKLSQLRSE FLVHRATYRV FGEKQWAEVQ GRLMVWRRSL ENVLGVLRTE RERFVRESLQ
AAAAAEEAAQ GKSNDKGNKS GDRRQRHGNN QQSQQQQQPQ EVAAAE