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Database: UniProt
Entry: G9N696_HYPVG
LinkDB: G9N696_HYPVG
Original site: G9N696_HYPVG 
ID   G9N696_HYPVG            Unreviewed;       868 AA.
AC   G9N696;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000256|HAMAP-Rule:MF_03002};
DE            Short=eIF3c {ECO:0000256|HAMAP-Rule:MF_03002};
DE   AltName: Full=Eukaryotic translation initiation factor 3 93 kDa subunit homolog {ECO:0000256|HAMAP-Rule:MF_03002};
DE            Short=eIF3 p93 {ECO:0000256|HAMAP-Rule:MF_03002};
DE   AltName: Full=Translation initiation factor eIF3, p93 subunit homolog {ECO:0000256|HAMAP-Rule:MF_03002};
GN   Name=NIP1 {ECO:0000256|HAMAP-Rule:MF_03002};
GN   ORFNames=TRIVIDRAFT_76057 {ECO:0000313|EMBL:EHK17658.1};
OS   Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS   (Trichoderma virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK17658.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK17658.1, ECO:0000313|Proteomes:UP000007115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
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:0000256|HAMAP-Rule:MF_03002}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03002}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03002}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000256|HAMAP-
CC       Rule:MF_03002}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHK17658.1}.
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DR   EMBL; ABDF02000088; EHK17658.1; -; Genomic_DNA.
DR   RefSeq; XP_013951856.1; XM_014096381.1.
DR   AlphaFoldDB; G9N696; -.
DR   STRING; 413071.G9N696; -.
DR   EnsemblFungi; EHK17658; EHK17658; TRIVIDRAFT_76057.
DR   GeneID; 25797807; -.
DR   VEuPathDB; FungiDB:TRIVIDRAFT_76057; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; G9N696; -.
DR   OMA; FRCGLIK; -.
DR   OrthoDB; 5482362at2759; -.
DR   Proteomes; UP000007115; 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: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: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:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR   PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR   Pfam; PF05470; eIF-3c_N; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03002};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_03002};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_03002}; Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT   DOMAIN          609..783
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..868
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          173..200
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        14..56
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   868 AA;  97849 MW;  82D698DA954A5698 CRC64;
     MSRFFRSGGD DSSSESSSDE EELYSGEEDQ ELDQEQSEEE SDEFDHSDEE SEDDDKEAGG
     DQKQGAFRFL RDNVASDSEG SDDEVRDKVK SAQVKRLDEL ETSIKQIENG QKNGDWTLIS
     TEFDKLNRQV TKLPAGSRIP KPYIKVIAEI EESVNEALAK AKVTPKKMNA TQARALNAVK
     QKVKKTNKDY QDEIAVYRED KDTYLWSSDE EEEVPQPKAP KAVKFDETAG ADEAADEGFA
     TVGKGGRTLQ YTPESIFKHL RGIMETRGKK NTDRLEQIKV MERLNEIANT PYQQIRVLLT
     LVSARFDLGS GTTNVMPLEH WKAAEKELSQ LLTILSQTSE YVVLENVEEW DDDEKPPTLQ
     PGEKHIKVAG SIVSYVERLD DELHRSLQSI DPHTSEYIER LQDEGALYNV IFRGLLYYEA
     LKKDETIEVP QDSVNRIVMR RLEHVYFKPA QVVKTFEENS WKAVGENVDS TTTPRAQAQD
     PTSLVNVLCA YLYANSEGIL RARALLSQVY FLALHDDYYK ARDMMLMSHL QETVTGFDIQ
     SQILYNRTLV QVGLCAFRKG LIYDAQNTLQ EICGSGRQKE LLAQGVMMQR YSQVSPEQER
     LEKQRQLPFH MHINLELLEC VYLTCSMLLE IPLLAQTGSS PDVKKRVISK TYRRMLEYHE
     RQIFTGPPEN TRDHVMQASK ALAAGEWKKS ITYIHSIKIW DLMPNTDEIK EMLSKQIQEE
     GLRTYLFTYA PFYDTLAIDT LSSMFELDST KVAAVISKMI SHEELAASLD QVTNNVIFRK
     GVELSRLQSL ALALSDKASA LIETNERTLE QRTQGTSSAF ERQGGRGRGG HRGGARGGRG
     GPRGGGNPQR QAGGTQFTGG ALGAAVRG
//
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