EIF3A_ASPFC
ID EIF3A_ASPFC Reviewed; 1051 AA.
AC B0XP13;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
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=AFUB_005560;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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; DS499594; EDP55856.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XP13; -.
DR SMR; B0XP13; -.
DR EnsemblFungi; EDP55856; EDP55856; AFUB_005560.
DR VEuPathDB; FungiDB:AFUB_005560; -.
DR HOGENOM; CLU_002096_2_1_1; -.
DR PhylomeDB; B0XP13; -.
DR Proteomes; UP000001699; 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 RNA-binding.
FT CHAIN 1..1051
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366352"
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
