EIF3A_ASPNC
ID EIF3A_ASPNC Reviewed; 1052 AA.
AC A2Q8I1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=An01g04430;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM269962; CAK36978.1; -; Genomic_DNA.
DR RefSeq; XP_001388870.1; XM_001388833.2.
DR AlphaFoldDB; A2Q8I1; -.
DR SMR; A2Q8I1; -.
DR PaxDb; A2Q8I1; -.
DR PRIDE; A2Q8I1; -.
DR EnsemblFungi; CAK36978; CAK36978; An01g04430.
DR GeneID; 4977231; -.
DR KEGG; ang:ANI_1_568014; -.
DR VEuPathDB; FungiDB:An01g04430; -.
DR HOGENOM; CLU_002096_2_1_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
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..1052
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366353"
FT DOMAIN 339..523
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 617..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 92..121
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 580..906
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 794..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 119864 MW; 10C1733FEDBD30CE CRC64;
MPPPPHIKPE NVLKRAQELI AVGQAPAALN VLHEHVTSKR TRSSPIASLE PVMLLFVELC
VDLRKGKAAK DGLYQYKNIA QNTNVGTIEV VLKKFIELAE KKVTEAQAKA DEIQSSLESA
APSSNVDDLE AIETPETILL ATVSGEQSRD RTDRAVVTPW LKFLWETYRT VLEILKNNAR
LEVMYQTTAL QAFQFCLKYT RKTEFRRLCE LLRNHVQNAA KYSAQMHAIN LSDPDTLQRH
LDTRFQQLNV AVELELWQEA FRSIEDIHTL LSLSKRPAKN VMMANYYEKL ARIFLVSENY
LFHAAAFSRY YNLLRQSAAA LAAGQGTKKE NPSVTEADMT KAASFVLLSA LSIPVISTSR
SRGALVDVDE VRKNKNTRLT NLLGMASPPT RAVLFKDALN KGLLKRARPE IRDLYNILEV
DFHPLSICKK ITPILKQIGA DPEMEKYVLP LQQVILTRLF QQLSQVYESV ELKFVYELAQ
FPDPFQITPS MIEKFIMNGC KKGDLAIRVD HISGVLTFDT DVFSSAKALH PGSAAGSAES
EVGSVQRLQN TPAEIARLQL TRLAKTLHVT CMYVDPSYNE ARLQAKRAAL ARAEAGAAKE
HEETLARRVI IEKKKEAATD ALQRKQREEE TRKRIRTQQL QEAEKQRLLD EHREREKKRI
KDEQDRIRQQ ELKKQLEELK TGVKGIDISE LDLNELDANR LRAMKLAQLE KEKNELNDRI
RTTAKRIDHL ERAFRREELK HVPEDYEKQK QRDMEIYEAT KAEALKEAED KHKEAVALKH
RLSRLVPQFN SFRKEVSEKR HEEFEKRRKA AERDFEAKKM QRIKEVQERR RRERAEREEE
ERRRKEEEER IRREEEERTA KEEERRRVLA EEKAKREEER KRLDELAAKQ KQREEEAEAR
RAARRTGGAE PEAAPERAAP TERTAPRLNL APRTGGAGPS WRERQAAKEA AGGTPAAPAA
AAPEPAREEP APVRRTGGYV PPHLRSGASA TPAAPAPAPS TERYVPRAMR EAGSSQPPSR
TQTPGSSSDK PEESKPAAGK WVPRWKQQQG GQ
