EIF3A_LODEL
ID EIF3A_LODEL Reviewed; 883 AA.
AC A5E1T3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=LELG_03570;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981527; EDK45391.1; -; Genomic_DNA.
DR RefSeq; XP_001525642.1; XM_001525592.1.
DR AlphaFoldDB; A5E1T3; -.
DR SMR; A5E1T3; -.
DR STRING; 379508.A5E1T3; -.
DR PRIDE; A5E1T3; -.
DR EnsemblFungi; EDK45391; EDK45391; LELG_03570.
DR GeneID; 5232466; -.
DR KEGG; lel:LELG_03570; -.
DR VEuPathDB; FungiDB:LELG_03570; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR InParanoid; A5E1T3; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR Proteomes; UP000001996; 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..883
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366364"
FT DOMAIN 327..505
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 803..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 101..133
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 547..862
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 803..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 102137 MW; 7FE00EAE68F8F187 CRC64;
MPPAHKGHAF RPENVLKRAR DLIGVGQKEA ALDTLYELII SKRIRYLQVE DLEPIADLLI
ELAVELRRGK LAKDALHQYK KNIQLNEHGL ESVQTIVRKF ISLAEKKLDE AQAQADIKID
QEEAAEEDLE TAQTPETILL SAVSNTDTAD RTERELVTPW LRFLWEAFRA TLDILRNNSK
LEVTYSAIVN QAFKFCLNFK RKAEFRRLCE LLRVHMQSVT TQTKTSSNNA IDLSDFETVQ
RYLEQRFAQL NIAVKLELWQ ESFRSVDDVH TLITASKKAP KPTMMANYYE NLARIFAVSD
NALFHAAAWN KFFNLYSQSP MATDEELKKY ASVFVLSTLA IPQSAIHDAD EHRTKNSKLS
SLLNLSQPPT KDGLTRSIIT RNVLKYVDEP IRILFELLQG GNFHPLSVKK QVVELFKILQ
ADENFKKYIP TLTEVILLRI FQQVSQVYDV VKLNFLTSLG VFEGLEYTLT ELEVEDLIVN
AVKDDLLALT IDHEAGVVNF KSNPFEETTT SFANDLQISP AELVRSQISK LAATLASSVQ
IIDPSYERRQ QEAKQAALQR AVEGLIREQQ RLADRTKILE ERKLAAEKRK REEEELQAKL
KQERIAAEQK AEQERLIQEQ ERKKEEKLQR EKEAILENEK RKLAEEINAK GIIKVDMNNL
KDLDKSKLQL MQIEQLNKDR KELEEKLKGT AKKADYLERA FRKYELKLLE AEAQKQQGLE
REQYENVKQL KVAKAKKDFD EAIQVRDRLQ RIIPDYTKFK SEIDAKNAVK VAKLKEEAQE
RFEKAKQERI EKVKRQRIEE LKSRKERERK AQAEEAARKA QAAEHAKLKE ELRIQREKDE
ELQRKRDEMA AAAAAAQAEQ EAKPPKQMSY SERMRLKREG KLP
