ID   EIF3A_ASPFU             Reviewed;        1051 AA.
AC   Q4WJQ1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   25-MAY-2022, entry version 89.
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 3 110 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
DE            Short=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03000};
DE   AltName: Full=Translation initiation factor eIF3, p110 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
GN   Name=tif32; ORFNames=AFUA_1G05200;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000007; EAL88231.2; -; Genomic_DNA.
DR   RefSeq; XP_750269.2; XM_745176.2.
DR   AlphaFoldDB; Q4WJQ1; -.
DR   SMR; Q4WJQ1; -.
DR   STRING; 746128.CADAFUBP00000546; -.
DR   EnsemblFungi; EAL88231; EAL88231; AFUA_1G05200.
DR   GeneID; 3507506; -.
DR   KEGG; afm:AFUA_1G05200; -.
DR   VEuPathDB; FungiDB:Afu1g05200; -.
DR   eggNOG; KOG2072; Eukaryota.
DR   HOGENOM; CLU_002096_2_1_1; -.
DR   InParanoid; Q4WJQ1; -.
DR   OMA; VMYQTTA; -.
DR   OrthoDB; 967904at2759; -.
DR   Proteomes; UP000002530; Chromosome 1.
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   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..1051
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   A"
FT                   /id="PRO_0000366351"
FT   DOMAIN          339..523
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          617..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          92..121
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          608..905
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COMPBIAS        794..907
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1008..1026
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1051 AA;  120229 MW;  53DDFFDF8D1A2F59 CRC64;
     MPPPPHIKPE NVLKRAQELI AVGQAPAALN VLHEHVTSKR TRSSPIASLE PVMLLFVELC
     VDLRKGKAAK DGLYQYKNIA QNTNVGTIEV VLKKFIELAE KKVTEAQAKA DEIQSSLESA
     APSSNVEDLE AIETPETILL ATVSGEQSRD RTDRAVVTPW LKFLWETYRT VLEILKNNAR
     LEVMYQTTAL QAFQFCLKYT RKTEFRRLCE LLRNHVQNAA KYSAQMHAIN LSDPDTLQRH
     LDTRFQQLNV AVELELWQEA FRSIEDIHTL LSLSKRPAKN VMMANYYEKL ARIFLVSENY
     LFHAAAWNRY YNLLRQSAAA LAAGQGTKKE NPSVTEADMT KAASFVLLSA LSIPVISTSR
     SRGALVDVDE ARKNKNARLT NLLGMAQPPS RAVLFRDALN KGLLKRARPE IRDLYNILEV
     DFHPLSICKK ITPILKQIGA DPEMEKYVLP LQQVILTRLF QQLSQVYESV ELKFVYELAQ
     FPDPFQITPA MIEKFIMNGC KKGDLAIRVD HTAGVLTFDT DIFSSAKALH SGSAAGSAES
     EVGSVQRLQN TPAEIARLQL TRLAKTLHVT CMYVDPSYNE ARIQAKKAAQ ARAEAGAAKE
     HEETLARRVL IEKKKEAATD ALQRKQREEE TRKRIRNQQL QEAEKQRLLD EQREREKKRL
     RDEQERIRQQ ELKKQLEELK SGVKGIDISE IDLEDLDANR LRAIKLAQLE KEKNELNERI
     RTTAKRIDHL ERAFRREELK HIPEDYEAQK KRDMELYEAI KAETLKEAEE KHKEAVALKH
     RLSRLVPVFS SFRKEVSEKR HEEFEKRRKA AEREFEAKKK QRIKEVQERR RRERAEREAE
     ERRRKEEEER AKREEEERIA KEEERRRILA EEKAKREEER KRLDEIAQRQ KQREEEAEAR
     RAARKSGLAE PPTRAAELER PVERTAPRLN LVSRTGSGPS WRERQAAKEA AGAAPAPAAA
     EAPKEEVQLP RRTGGYVPPH LRSGANASPA TPPSNGPAPE KYVPRHMRES SSSQPPSRTQ
     TPPAAAPASS DKPEASPAPQ KWVPRWKQQQ Q