ID   EIF3A_MAIZE             Reviewed;         962 AA.
AC   Q9XHR2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=eIF-3-theta {ECO:0000255|HAMAP-Rule:MF_03000};
GN   Name=TIF3A1; Synonyms=IF3A;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. LG11; TISSUE=Root tip;
RX   PubMed=10394920; DOI=10.1007/s004380050026;
RA   Sabelli P.A., Burgess S.R., Valasek L., Shewry P.R.;
RT   "Molecular cloning and characterisation of a maize cDNA for a homologue of
RT   the large subunit of the eukaryotic initiation factor 3 (eIF3).";
RL   Mol. Gen. Genet. 261:820-830(1999).
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; AF073329; AAD39834.1; -; mRNA.
DR   RefSeq; NP_001105726.2; NM_001112256.2.
DR   AlphaFoldDB; Q9XHR2; -.
DR   SMR; Q9XHR2; -.
DR   STRING; 4577.GRMZM2G093050_P02; -.
DR   PaxDb; Q9XHR2; -.
DR   PRIDE; Q9XHR2; -.
DR   GeneID; 542747; -.
DR   KEGG; zma:542747; -.
DR   eggNOG; KOG2072; Eukaryota.
DR   OrthoDB; 967904at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q9XHR2; baseline and differential.
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; 1.
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..962
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   A"
FT                   /id="PRO_0000123541"
FT   DOMAIN          316..511
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          814..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          92..123
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          555..755
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          790..860
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COMPBIAS        814..857
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        943..962
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   962 AA;  111564 MW;  436E9B8658921E76 CRC64;
     MATFAKPENA LKRAEELIHV GQKQSALQAL HDLITSKRYR SWQKPLEKIM MKYVELCVDL
     RKGRFAKDGL IQYRIVCQQV NVSSLEDVIK HFMQLSNEKA EQAKSQVEAL EDALDVEDLE
     ADKRPEDLML SFVSGEKGKD RSDKEVVTPW FKFLWETYRT VLEILRNNSK LEALYAMTAH
     RAFQFCKQYK RTTEFRSCVR SIRNHLANLN KYRDQRDRPD LTAPESLQLY LDTRVEQLKV
     ATELSLWQEA FRSVEDIHGL MTMVKKMPKP SILVVYYAKL TEIFWISDSH LYHAYAWLKL
     FNLQKSYNKN LSQKDLQLIA SSVLLAALSV SPYDKKYGAF ETENEKERNM RLSNLVNFSL
     DNKRENREMP SRPYLLSELA SKGVLSCASQ EVRDLYNLLE HRFLPLDLAS KVQPLLLKIS
     KIGGKLSSAS SVPEVKLSQY ISALEKLTTL RVLQQASCIF KSIKIDMLSR MIPFFDFSVV
     EKISVDAAKQ NFVAIKVDHL SGVVQFGTVD IESDGLSDHL SVLADSLNKA RIHICPPVKK
     PSKLGESLIS LAAIVENEHK RLLARKSIIE KRKEELERQI LEKEKEEEKK RMSSQKKTVD
     EERVRLLNEQ RQREQDRIRR EIEEKNKAEA KKMLEDLNKA GKKHVVVEGE LTKEAYMELA
     RNEQLKERHE MEKKLQKFAK TMDYLERAKR QEEAPLIEQA FQKRLEEEKI LHEQEQLREI
     ELSKQHHASD LQEKNRLSRM LEHKNALQER IIQERAAEFG RLKKERDERM NRLISSRKHE
     RETVRKLMFY LNLEEQRIEM LREEEEARKR EAEERRKREE AERKAKLDAI AEKQRLREIE
     LEEKAKATRE KLLKGSEAVR APDSAPVAQP PRESAAAAAA AAAAAPAPSK YIPKFKRGGD
     SSSIPSGSRD EDRWGSRGPL RQDGPPARLD APSSRQDTDR WRGSRFPSNS TSSSSTWSRS
     RN