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EIF3A_CANGA
ID   EIF3A_CANGA             Reviewed;         951 AA.
AC   Q6FK21;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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};
GN   OrderedLocusNames=CAGL0M01804g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380959; CAG62399.1; -; Genomic_DNA.
DR   RefSeq; XP_449423.1; XM_449423.1.
DR   AlphaFoldDB; Q6FK21; -.
DR   SMR; Q6FK21; -.
DR   STRING; 5478.XP_449423.1; -.
DR   EnsemblFungi; CAG62399; CAG62399; CAGL0M01804g.
DR   GeneID; 2891193; -.
DR   KEGG; cgr:CAGL0M01804g; -.
DR   CGD; CAL0136403; CAGL0M01804g.
DR   VEuPathDB; FungiDB:CAGL0M01804g; -.
DR   eggNOG; KOG2072; Eukaryota.
DR   HOGENOM; CLU_002096_2_1_1; -.
DR   InParanoid; Q6FK21; -.
DR   OMA; VMYQTTA; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR   GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
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   GO; GO:0002188; P:translation reinitiation; IEA:EnsemblFungi.
DR   HAMAP; MF_03000; eIF3a; 1.
DR   InterPro; IPR027512; EIF3A.
DR   InterPro; IPR000717; PCI_dom.
DR   PANTHER; PTHR14005; PTHR14005; 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..951
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   A"
FT                   /id="PRO_0000366357"
FT   DOMAIN          298..496
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          503..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          863..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          97..125
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          496..532
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          592..676
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          704..779
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COILED          808..909
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT   COMPBIAS        504..540
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..906
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   951 AA;  110157 MW;  DC6B47AEBB351A5A CRC64;
     MAPPPLRPEN ALKRADELIS VNEKPAALQS LYEFITARRI RYATPSQVEP IVFKFLELGV
     ELKKGKLIKD ALYQYKKLVH GSAEGLVSVG AVLRKFIDYV ETKLASEQAK AEEKQKEEVS
     DDLEGGVTPE NLLSSVYEAD HSVAGFNDEA LNSWMRFSWE SYRTALDLLR NNSQLEITYS
     GVVSRTMQFC LKHQRKNEFK RLAEMLRQHL DTANYHQSKF GSNQVDLSDA DTLQRYLDQR
     FQLVDASVKL GLWHEAYKAA EDVYHLMKMT TRKPKSSTLA NYFENLVQIF LVSGDQILHT
     LAWKKYFELY STNPNATEEE FKKIASTIFL SALSIQLDDL PNVRYNYQSR SYRLLDVETK
     PTRKEVIQSI VEDDTIFSRV DAETKTLYEI MEVEFDGESF KGKFEAILPK LEGESYFANY
     SVSLRDVIIR RMFVFASQKY EDISLNDLYS SVTFSSSFKL SEWDIEKQLL QAAVDDYVSF
     QLDHEQNKVT FVKDPLVNFA AIKEEEVEEE EEEEEEEEEE EKEAEGAEGA EGDTEEGQEA
     VAEPEPVIKR NYYIRKRLSE LYEKLLEDTD YNTVSYLDKV RIAREALIKH TKDTIEDMKK
     NSEERAKMHQ ERRRQHMESA AMNAEKDAEQ RQKRIMEERA SIEAKLEEEA HRRLIEKKKR
     EFEEVKQREI RKLVDELNAK GNGTKVEYDE VKDMDIPDIT KYFVNRLSKN KDELEERMNF
     AVKRMDHLER AYRKVELPLL KKQADELRAT DEVNFGNMKK KIVDAAKAEY EAKMEDYNRV
     SSVFDDYKTL RDRMLAAHNE KFAAIRAENA AKLEAAKKAR IEEVRKQRYE ELLARSEAEK
     KAAEEAERRA KLDEIARKQR EMEEALERKS AARTFTQPRA PVVPNANLDE IARKQREMEE
     AIERKLAGKS AAPAPAPAPA ASTPAASTPA APGKMSFAER MRLKRQQQQQ K
 
 
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