EIF3A_MAGO7
ID EIF3A_MAGO7 Reviewed; 1073 AA.
AC A4RM69; G4MUP2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=MGG_10192;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001232; EHA54015.1; -; Genomic_DNA.
DR RefSeq; XP_003713822.1; XM_003713774.1.
DR AlphaFoldDB; A4RM69; -.
DR SMR; A4RM69; -.
DR STRING; 318829.MGG_10192T0; -.
DR PRIDE; A4RM69; -.
DR EnsemblFungi; MGG_10192T0; MGG_10192T0; MGG_10192.
DR GeneID; 2681764; -.
DR KEGG; mgr:MGG_10192; -.
DR VEuPathDB; FungiDB:MGG_10192; -.
DR eggNOG; KOG2072; Eukaryota.
DR HOGENOM; CLU_002096_2_1_1; -.
DR InParanoid; A4RM69; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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..1073
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000366365"
FT DOMAIN 338..522
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 798..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 596..737
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 790..910
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 798..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1073 AA; 122137 MW; F25BD4933BCF0C56 CRC64;
MPPPPHQKPE NVLKRAHELI GVNQAPAALT LLHEHITSKR SRNVPIASLE PVMVLLVELS
VEQKKGKLAK DALYQYKNIA QNTNVGTIEL VLKKFIELAA GKVTAAQQKA DEVQSSIEAT
NSTSVDDLEA TETPESILLA TVSGEQSRDR TDRAIVTPWL KFLWEAYRTV LDILRNNARL
ELLYQSTAMQ AFEFCLKYIR KTEFRRLCEL LRNHVQTAAK YSTQMHAINL NDPDTLQRHL
ETRFQQLNVA VELELWQEAF RSVEDIHTLL NLSKRPPKNI MMANYYEKLT RIFLVGENYL
FHAAAWSRYY SLLRQSAAVV ASGQGKKADN PPATPADLQK AASFVLLSAL SIPVISTTRS
RGAMVDFDEA KKNKNSRLTH LLNMSQAPTR AVLFKDAMSK SLLNQARPEI RDLYNILEVD
FHPLSICKKI SPILAQIGAD EDMKKYVLPL QQVILTRLFQ QLSQVYETVD LEFVESLAQF
PEPFQVTRAT VEKFIMNGNK KGDLSIRMDH GTGVLSFDTD IFSSSKASHS GSAAGSAEAE
GGSVQRLQRT PSEIVRSQLV RLGRALYTTC YYVDPSFNES RVKAREAALA RAKAGAEKEH
REILARKDII QKRKEEASDL QAKREKENAK IKRMREQALL EAEQQRLAEE QKERERKRKE
KEMQEIRKQE AESLIKDLKI GPNALDVSAE DLANLDTSQI RAIKVAQLER EKNDINEKLR
ITGKRLDHLE RAYRKEEVKK LHEDYESQKK RDLDAYSKIK EETLKESKIK HEESVELKHR
LSRLMPFYEE FRANLQERRR DEFEKRRRDA ERELEKQIAQ RKKEYREKKL REKRQREEEE
RQLREAEERA AKEKEEQKRR EEARKEELAR AKAQREAERQ EMAEKAALQA RREEEALERR
KREKEKLASA PPASAAPVRA SESAGGPPRL NLAGAGGKPS WRDRVPSSNV GAAPSERSER
PSERPAPART GTPMERTDSN DRAGGPPRLN LARADGAKPS WREREQAKAS GGPERDLPPS
RAASGRGPPM HRTDSGRGEN GRDESPAPPR DSLTASGAPG KYVPRWKREN AGN
