ID   EIF3A_TOBAC             Reviewed;         958 AA.
AC   Q40554;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE            Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE   AltName: Full=Eukaryotic translation initiation factor 3 large subunit;
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 10 {ECO:0000255|HAMAP-Rule:MF_03000};
DE   AltName: Full=PNLA-35;
DE   AltName: Full=eIF-3-theta {ECO:0000255|HAMAP-Rule:MF_03000};
GN   Name=TIF3A1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. SR1; TISSUE=Leaf;
RA   Borisjuk N., Sitailo L.;
RL   Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with other
CC       initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC       the 40S 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_03000}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03000}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC       Rule:MF_03000}.
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DR   EMBL; X79794; CAA56189.1; -; mRNA.
DR   PIR; S47179; S47179.
DR   RefSeq; NP_001311594.1; NM_001324665.1.
DR   AlphaFoldDB; Q40554; -.
DR   SMR; Q40554; -.
DR   STRING; 4097.Q40554; -.
DR   GeneID; 107760201; -.
DR   KEGG; nta:107760201; -.
DR   Proteomes; UP000084051; Unplaced.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IBA:GO_Central.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR   GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR   GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR   HAMAP; MF_03000; eIF3a; 1.
DR   InterPro; IPR027512; EIF3A.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR14005; PTHR14005; 2.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..958
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   A"
FT                   /id="PRO_0000123542"
FT   DOMAIN          316..513
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          804..958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          93..123
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          548..696
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          796..861
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COMPBIAS        804..861
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        925..944
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   958 AA;  111615 MW;  C971810583DEDBC7 CRC64;
     MATFAKPENA LKRAEELITV GQKQEALQAL HDLITSRRYR AWQKTLERIM FKYVELCVDM
     RRGRFAKDGL IQYRIVCQQV NINSLEEVIK HFMHLATERA ELARNQAQAL EEALDVEDLE
     ADKRPEDLML SYVSGEKGKD RSDRELVTPW FKFLWETYRT VLEILRNNSR LEALYAMTAH
     RAFQFCKQYK RTTEFRRLCE IIRNHLANLN KYRDQRDRPD LSAPESLQLY LDTRFEQLKV
     ATELGLWQEA FRSIEDIYGL MCMVKKTPKA SLMVVYYGKL TEIFWMSSNH LYHAYAWLKL
     FSLQKSFNKN LSQKDLQLIA SSVVLAALSV PPYDQSYGAS HLELENEKER SLRVANLIGF
     EVEPKAENRV ALSRSSLLSE LVSKGVMSCV TQEVKDLYHL LENEFLPLDL ALKVQPVLSK
     ISKLGGKLSS VSSVPEVQLS QYVPALEKLA TLRLLQQVSQ VYQTIQIDNI SKMIPFFDFT
     VIEKISVDAV RRNFLAIKVD HMKGLSSLVN RVLRRKDSGI ICLFLAESLS KARTMIYPPA
     KKAAKLGEAL SNLAEIVEKE HKRLLARKSI IEKRKEEQER LLLEMERVEE TKRRDVQKMT
     EEAEQKRIAA EYEQRRNQRI LKEIEDRELE EAQALLHEAE KRSKRKKKPV LEGEKMTKKV
     IMELALNEQL RERQEMEKKL LKFAKSMDHL ERAKREEAAP LIESAFKQRL AEEAALHERE
     QQQEIELSRQ RHAGDLEEKR RLARMLENKR ILQEKVVSSR EAEFTRMKRE RQERISQIIQ
     SRKQEREARR KMIFFLRSEE ERQKRLQEEE EARKREEAER RKKEEAERQA KLDEIAEKQR
     RRMLELEEKE KREREEILRK STAVLPKPAE PPTLGRPAEL GGAAPIPAAA ATAPTPGPGK
     YVPKHLRTKM DGAGQAPPPE TDKWGGGSKP DDRPSWRDER KPPSFGSGSR TSWPASRR