EIF3A_ASPOR
ID EIF3A_ASPOR Reviewed; 1038 AA.
AC Q2UKG6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=AO090003000816;
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: 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; AP007155; BAE57949.1; -; Genomic_DNA.
DR RefSeq; XP_001819951.1; XM_001819899.2.
DR AlphaFoldDB; Q2UKG6; -.
DR SMR; Q2UKG6; -.
DR STRING; 510516.Q2UKG6; -.
DR EnsemblFungi; BAE57949; BAE57949; AO090003000816.
DR GeneID; 5991934; -.
DR KEGG; aor:AO090003000816; -.
DR VEuPathDB; FungiDB:AO090003000816; -.
DR HOGENOM; CLU_002096_2_1_1; -.
DR OMA; VMYQTTA; -.
DR Proteomes; UP000006564; Chromosome 2.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; 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_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..1038
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366354"
FT DOMAIN 339..523
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 621..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 92..121
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 611..899
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 800..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 118341 MW; 00A7A6BD44A540C9 CRC64;
MPPPPHIKPE NVLKRAQELI AVGQAPAALN VLHEHVTSKR TRSSPIVSLE PVMLLFVELC
VDLRKGKAAK DGLYQYKNIA QNTNVATIEV VLKKFIELAE KKVTEAQAKA DEIQSSLESA
APSSNVEDLE AIETPETILL ATVSGEQSRD RTDRAVVTPW LKFLWETYRT VLEILKNNAR
LEVMYQTTAL QAFQFCLKYT RKTEFRRLCE LLRNHVQNAA KYSAQMHAIN LSDPDTLQRH
LDTRFQQLNV AVELELWQEA FRSIEDIHTL LSLSKRPAKN VMMANYYEKL ARIFLVSENY
LFHAAAWSRY YNLLRQSAAT LAAGQGTKKE NPSVTDADMT KAVSFVLLSA LAIPVISTSR
SRGALVDVDE VRKNKNTRLT NLLGMAQSPT RAVLFKDALN KGLLKRARPE IRDLYNILEV
DFHPLSICKK ITPILKQIGA DPEMEKYVVP LQQVILTRLF QQLSQVYESV SLKFVYELAQ
FPDPFQVTPA MIEKFIMNGC KKGDLAIRVD HISGVLTFDT DVFSSAKALH SGSAAGSAES
EVGSVQRMQN TPAEIARLQL TRLAKTLHVS CMYVDPSYHE ARLQAKQAAQ TRAAAGAAKE
HEETLARRVI IDKKKEAATD ALQRKQREEE TRKRIRTQQL QEAEKQRLLD EQREREKKRI
KDEQDRIREQ ELKKQIEELK SGVKGIDLSE VDLKDLDANR LRAMKLAQLE KEKNELNDRI
RTTGKRIDHL ERAFRREELK HIPADYEAQK KRDMELYEAL KAETLKEAED KHKEAVALKH
RLSRLVPVFN NFRKEVSEKR HEEFERRRKA AERDFEAKKK QRIKEVQDRR RRERAEREEA
ERRQKEEEER IKREEEERAA KEEERRRVLA EEKAKREEER KKLDEIALKQ KQREEEAEAR
RASRKTGFPE PPARAEPERT APRLNLAPRT GGGPSWRERQ AAKEAAGGAA PEPAKEEPAA
QPPRRTGGYV PPHLRGASAA APAAPPSNGA APSRYVPPSA RDSGSSTPPS RTQTPATTSE
EPKSAGKWVP RWKQQQGQ
