EIF3A_ASPCL
ID EIF3A_ASPCL Reviewed; 1044 AA.
AC A1CRE5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=ACLA_029440;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027059; EAW08216.1; -; Genomic_DNA.
DR RefSeq; XP_001269642.1; XM_001269641.1.
DR AlphaFoldDB; A1CRE5; -.
DR SMR; A1CRE5; -.
DR STRING; 5057.CADACLAP00001793; -.
DR PRIDE; A1CRE5; -.
DR EnsemblFungi; EAW08216; EAW08216; ACLA_029440.
DR GeneID; 4700907; -.
DR KEGG; act:ACLA_029440; -.
DR VEuPathDB; FungiDB:ACLA_029440; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR Proteomes; UP000006701; 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..1044
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366350"
FT DOMAIN 339..523
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 797..1044
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..907
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 797..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1044 AA; 118946 MW; 943D6E5120963353 CRC64;
MPPPPHIKPE NVLKRAQELI AVGQAPAALN VLHEHVTSKR TRSTPIVSLE 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 NPSVTDADMT KAASFVLLSA LSIPVISTSR
SRGALVDVDE VRKNKNTRLT NLLGMAQAPS RAVLFRDALN KGLLKRARPE IRDLYNILEV
DFHPLSICKK ITPILKQIGA DPEMEKYVLP LQQVILTRLF QQLSQVYESV ELKFIYELAQ
FPEPFQVTPA MIEKFIMNGC KKGDLAIRVD HISGVLTFDT DIFSSAKALH PGSAAGSAES
EAGSVQRLQN TPAEIARLQL TRLAKTLHVT CMYVDPSYSE VRIQAKQAAQ ARAAAGVAKE
HEETLARRVI IDKKKEAATD ALQRKQREEE TRKRIRTQQL QEAEKQRLLD EQREREKKRI
KDEQDRIRQQ ELKKQLEELK SGVKGIDISE LDLEDLDANR LRAIKLAQLE KEKNELNDKI
RTTAKRIDHL ERAFRREELK HIAEDYEAQK QHDMEVYEAT KAETLKEAKE KHAEAVALKH
RLSRLVPVYS NFRKEVSEKR HEEFEKRRKA AERDFEAKKK QRIREVQERR RRERAEREAE
EQRQKEEEER ARREEEERVA REEERRRVLT EEKAKREEER KKLDEIALKQ KQREEEAEAR
RAARKAGVTE PPPRAAEPER TAPRLNIAPR TGGSSWRERQ AAKEAAGGAA PAAAPAPEAP
KEEAQPPRRT GGGYVPPHLR SGAGASAAPA APPATEKYVP RHMRDSSSSQ PPSRTQTPPA
PAAEKPEGSG APQKWVPRWK QQQS
