EIF3A_ASPTN
ID EIF3A_ASPTN Reviewed; 1040 AA.
AC Q0CUP6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=ATEG_02588;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476596; EAU37550.1; -; Genomic_DNA.
DR RefSeq; XP_001211766.1; XM_001211766.1.
DR AlphaFoldDB; Q0CUP6; -.
DR SMR; Q0CUP6; -.
DR STRING; 341663.Q0CUP6; -.
DR PRIDE; Q0CUP6; -.
DR EnsemblFungi; EAU37550; EAU37550; ATEG_02588.
DR GeneID; 4317119; -.
DR VEuPathDB; FungiDB:ATEG_02588; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR Proteomes; UP000007963; 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..1040
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366355"
FT DOMAIN 339..523
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 617..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..1040
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..906
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 795..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 118858 MW; 03888EA6A6E829E0 CRC64;
MPPPPHIKPE NVLKRAQELI AVGQAPAALN VLHEHVTSKR TRSSPISSLE PVMLQIVELC
VDMRKGKAAK DGLYQYKNIA QNTNVGTIEV VLKKFIELAE KKVTEAQTKA DEIQSSLESA
APSANVEDLE AIETPETILL ATVSGEQSRD RTDRAVVTPW LKFLWETYRT VLEILKNNAR
LEVMYQTTAL QAFQFCLKYT RKTEFRRLCE LLRNHVQNAA KYSAQMHAIN LSDPDTLQRH
LDTRFQQLNV AVELELWQEA FRSIEDIHTL LSLSKRPAKN VMMANYYEKL ARIFLVSENY
LFHAAAWSRY YNLLRQSAAT LAAGQGTKKE NPSVTEADMT KAASFVLLSA LAIPVISTSR
SRGALVDVDE VRKNKNTRLT NLLGMAQPPT RAVLFKDAMN KGLLKRARPE IRELYNILEV
DFHPLSICKK ITPILKQIGS DPEMEKYVVP LQQVILTRLF QQLSQVYESV ELKFVYELAQ
FPDPFQITPA MIEKFIMNGC KKGDLAIRVD HISGVLTFDS DVFSSAKALH PGSAAGSAES
EVGSVQRLQN TPAEIARLQL TRLAKTLHVS CMYVDPSYNE SRIQAKQTAQ ARALAGAAKE
HEETLARRVI IEKKKEAATD ALQRKQREEE TRKRIRTQQL QEAEKQRLLD EQREREKKRI
KDEQDRIRQQ ELKKQLEELK SGVKGIDINE IDLQDLDANR LRAMKLAQLE KEKNELNDRI
RTTGKRIDHL ERAFRREELK HIPEDYEAQK KRDMEIYEAT KAETLKEAEL KHKEAVALKH
RLSRLVPHFN SFRKEVSEKR HEEFEKRRKA AERDFEAKKK QRVKEVQERR RREKMEREMA
ERQRKEEEER AQREEEEKRA RDEERRRVLA EEKAKREEER KRLDEIAAKQ KQREEEAEAR
RAARKAGLEP AAPAARPEPT ERTAPRLNIA PRTGGPSWRE RQAAKEAAGG AAPEAAPKEE
APQPARRPGG YVPPHLRSGS SAAPAAPPSN GAPERYVPRH ARESSSSQPP SRTQTPGSDK
PSEGGSAGKW VPRWKQQQNQ
