EIF3A_NEOFI
ID EIF3A_NEOFI Reviewed; 1067 AA.
AC A1D4A7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=NFIA_019540;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW23250.1; -; Genomic_DNA.
DR RefSeq; XP_001265147.1; XM_001265146.1.
DR AlphaFoldDB; A1D4A7; -.
DR SMR; A1D4A7; -.
DR STRING; 36630.CADNFIAP00002086; -.
DR EnsemblFungi; EAW23250; EAW23250; NFIA_019540.
DR GeneID; 4590839; -.
DR KEGG; nfi:NFIA_019540; -.
DR VEuPathDB; FungiDB:NFIA_019540; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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..1067
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366366"
FT DOMAIN 339..523
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 617..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..1067
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..899
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 795..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 121373 MW; 29B185EFF0EED240 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 YNLLRQSAVA LAAGQGTKKE NPSVTEADMT KAASFVLLSA LSIPVISTSR
SRGALVDVDE ARKNKNTRLT NLLGMAQPPS RAVLFRDALN KGLLKRARPE IRDLYNILEV
DFHPLSICKK ITPILKQIGA DPEMEKYVLP LQQVILTRLF QQLSQVYESV ELKFVYELAQ
FPDPFQITPA MIEKFIMNGC KKGDLAIRVD HTSGVLTFDT DIFSSAKALH SGSAAGSAES
DVGSVQRLQN TPAEIARLQL TRLAKTLHVT CMYVDPSYNE ARIQAKKAAQ ARAEAGAAKE
HEETLARRVL IEKKKEAATD ALQRKQREEE TRKRIRTQQL QEAEKQRLLD EQREREKKRL
KDEQDRIRQQ ELKKQLEELK SGVKGIDISE IDLEDMDANR LRAIKLAQLE KEKNELNERI
RTTAKRIDHL ERAFRREELK HIPEDYEAQK KRDMELYEAI KAETLKEAEE KHKEAVALKH
RLSRLVPVFS SFRKEVSEKR HEEFEKRRKA AEREFEAKKK QRVKEVQERR RREKAEREAE
ERRRKEEEER AKREEEERIA KEEERRRVLA EEKAKREEER KRLDEIALRQ KQREEEAEAR
RAARKSGLAE PPTRAAEPER PAERTAPRLN LASRTGGAPS WRERQAAKEA TGAAPAPAPV
PAPAAAPAAA PAPAAEAPKE EVQLPRRTGG YVPPHLRSGA SASPAAPPSN GPAPEKYVPR
HMRESSSSQP PSRTQTPPAP AAAASSDKPE GSPAPQKWVP RWKQQQQ
