EIF3A_VANPO
ID EIF3A_VANPO Reviewed; 942 AA.
AC A7TL64;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
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 {ECO:0000255|HAMAP-Rule:MF_03000}; ORFNames=Kpol_1065p43;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480412; EDO17027.1; -; Genomic_DNA.
DR RefSeq; XP_001644885.1; XM_001644835.1.
DR AlphaFoldDB; A7TL64; -.
DR SMR; A7TL64; -.
DR STRING; 436907.A7TL64; -.
DR EnsemblFungi; EDO17027; EDO17027; Kpol_1065p43.
DR GeneID; 5545199; -.
DR KEGG; vpo:Kpol_1065p43; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR InParanoid; A7TL64; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR PhylomeDB; A7TL64; -.
DR Proteomes; UP000000267; 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..942
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366370"
FT DOMAIN 320..494
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 502..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 499..529
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 588..669
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 705..734
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 821..912
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 504..539
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..870
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 942 AA; 108577 MW; F328DF74C2815BD9 CRC64;
MAPPVLRPDN AIKRADELIS VGESQAALQS LYEYLTARKI RFAQPSTVEP IVFKFLELGV
DLKRGRLIKD ALHQYKKLVQ GSQDGLSSVG AVARKFIDCV ETKMAFEHLK AEESQTEEDD
DLEGGVTPEN LLKSVYIQDQ SVAGFNDEVV TSWLKFTWES YRAVLDLVRN NSQLEITYAG
VVNRTMQFCL KYNRKNEFKR LAEMLRQHLD AANYQQSKIG SNIVDLSDSE TLQRYLDQRF
LQLNVSVKLE LWHEAFRSIE DVYHLMKMSK HTPKSSTLAN YYENLAKVFL ISNAQLLHTA
TWEKFYRLYQ SNPNATEEDF KKYSSIILLS ALSTPLDILP TVGYDPQMRL YRLLGLESRP
TRNEMIELAK QEDIYKHIDE DIIKLYEIME INYNADTIKT EIAALLPKLE AKPYFKQYIN
QLRNVLLRKN YVSLSETENA IPTDALYDKA SLPGVLSLPH WDMEKTLLQA AVEDYVSISI
DHDSNTVTFF KDPFEIISKA AGTVEEEEEE EEEEGEEVEG EEAETGEEIV EEGEEHENEE
NKEPEPVITR TTFIRNRLAE LSNVLEEIDA FKNASYLEKV KLARETLITQ TKDSIENLKQ
IAEDRAKRAQ EQKKKYMASA AVRAEEDAEI RQRQILEEKA ALEAKLEQDA HRRLVEKKKR
EFEDLKQREI QKFIDEFNKK DHAAKIASEE VQGLDIKEIK TLIFSKLSQD KSELEDRMTS
SLQKLDHAER AYRKSELPLL RKEAESLKET DMNKFNDMKS KIVDTARAEF DAKMEDHNRL
VGVYNDYVSL KDRLTTTVEE KFKLIRAENA AKFEAAKKAR IEEVRKQRYE ELVAERKAEI
EAEEREERAK KQEETARKQK EMEEAAERKS KASSAAAAKS ILTGGNDARS AKLDEIARRQ
REIEQAAERK AQGPSASTEA PDDEGRNLTY AEKMKLRRAS KK
