ID   EIF3C_MAGO7             Reviewed;         865 AA.
AC   A4QSX4; G4N5D3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002};
DE            Short=eIF3c {ECO:0000255|HAMAP-Rule:MF_03002};
DE   AltName: Full=Eukaryotic translation initiation factor 3 93 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03002};
DE            Short=eIF3 p93 {ECO:0000255|HAMAP-Rule:MF_03002};
DE   AltName: Full=Translation initiation factor eIF3, p93 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03002};
GN   Name=NIP1 {ECO:0000255|HAMAP-Rule:MF_03002}; ORFNames=MGG_05243;
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: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis of a
CC       specialized repertoire of mRNAs and, together with other initiation
CC       factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC       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_03002}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03002}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000255|HAMAP-
CC       Rule:MF_03002}.
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DR   EMBL; CM001233; EHA52990.1; -; Genomic_DNA.
DR   RefSeq; XP_003712797.1; XM_003712749.1.
DR   AlphaFoldDB; A4QSX4; -.
DR   SMR; A4QSX4; -.
DR   STRING; 318829.MGG_16895T0; -.
DR   EnsemblFungi; MGG_16895T0; MGG_16895T0; MGG_16895.
DR   GeneID; 12985729; -.
DR   KEGG; mgr:MGG_16895; -.
DR   VEuPathDB; FungiDB:MGG_16895; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; A4QSX4; -.
DR   OMA; VVMHRSE; -.
DR   OrthoDB; 273138at2759; -.
DR   Proteomes; UP000009058; Chromosome 3.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:EnsemblFungi.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:EnsemblFungi.
DR   GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:EnsemblFungi.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_03002; eIF3c; 1.
DR   InterPro; IPR027516; EIF3C.
DR   InterPro; IPR008905; EIF3C_N_dom.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13937; PTHR13937; 1.
DR   Pfam; PF05470; eIF-3c_N; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..865
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000364285"
FT   DOMAIN          606..780
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..52
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   865 AA;  97070 MW;  60C5EBE7D65D7A95 CRC64;
     MSRFFRGGNE SSSESSSDEE ELYSEEEEEE LEDEGDDSDN DGSGDDDSDS DSDADAGGKK
     KGAAKFLVDD DSSDEEDSDA EVTTKVKSAK DKRLDELEST VTAIANGMKI NDWGSIATEF
     DKLNRQAEKL RTGTTAPKMY IKSIADLEDF MNETLAKQKV TPKKMNATNA RGLNAVKQRI
     KKNNKEYQAQ IDAYKADEFE FMMDTEDEEE PAPKPKKAAK VSFDEATAED EEDDEGFARV
     GKGGKTLQFT PESIFKHLRS ILESRGKKNT DRGEQIKIME KLGEIAQTPY QRIRVLLALV
     SSRFDIGTSA GAALSVEHWK AAEKELSLLL TVLDENKDHI VLESAEEWDD DEKPPTLEKG
     EKYIKIPGSI VSYTERLDDE LTRSLQAIDP HTSEYIDRLS DEGALYNIIF RAQLYYEGLR
     KDASLEIPQE SLNRAIMRRL DHVYFKPAQV IKILEENSWK AVGDKASNIT PREQTVEAAQ
     LVNVLCNYLF ANSEGIHRAR AMLCQIYFLA LHDDYYKSRD MMLMSHLQET ISSFDVLTQI
     LYNRTLVQVG LCAFRKGLVY DAQNTLQDIC GSGRQKELLA QGVMIQRFNQ VSPEQERLER
     QRQLPFHMHI NLELLECVYL TCSMLLEIPL LAQTGSSPDI KKRIISKTYR RMLEYHERQI
     FTGPPENTRD HVMQASKALA AGEWKKATSF IHSIKIWELM PNADAIKTML AKQIQEEGLR
     TYLFTYAPFY DTLSIETLSN MFELESTKIS AVVSKMISHE ELAAALDQVK QTVIFRKGVE
     LSRLQSLALT LSDKASSLIE SNERTLEQRT QGTSNAFERQ GGRGGRGGGR GRGGGRGGPR
     FGGNTQRQAG GTQFTGGALG AAVRA