ID   EIF3C_SCLS1             Reviewed;         870 AA.
AC   A7E471;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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; ORFNames=SS1G_00093;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(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: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; CH476621; EDN90693.1; -; Genomic_DNA.
DR   RefSeq; XP_001598007.1; XM_001597957.1.
DR   AlphaFoldDB; A7E471; -.
DR   SMR; A7E471; -.
DR   STRING; 665079.A7E471; -.
DR   EnsemblFungi; EDN90693; EDN90693; SS1G_00093.
DR   GeneID; 5494678; -.
DR   KEGG; ssl:SS1G_00093; -.
DR   VEuPathDB; FungiDB:sscle_03g029750; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; A7E471; -.
DR   OMA; VVMHRSE; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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..870
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000366885"
FT   DOMAIN          608..782
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          807..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..53
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   870 AA;  97816 MW;  8ED8797457D113A3 CRC64;
     MSRFFRGDSS SESSSDEEED LYSDDEEVQE QPEEESEEDD SEEDDDDDDS DSSSDDGVGK
     KTGANAFLKD DSDSDSESSG DEGVKVVKSA KNKRFEELEA TAKAIENGEK INDWGSISAE
     FDKLNRQVAK LLQSGTTPKV YIKALAELED FMNETLAKQK VTPKKMNATN SRGLNAVKQK
     LKKTSKEHQK DIDSFRADKD AYMESEDEEV VAPKPKKAKS SAAAQNLVID GDDDEGWGTV
     GKGGRTLQFT PESILKHLRT ILESRGKKNT DRNEQIKIME KLYEVAATPY QRIRVLLTLI
     STRFDMTTGT QTFMSQEQWK AAEKEFATLL SVVETNREFV VVETAEPWED DEKLPTVADG
     EKFKIPGSIV SFVERLDDEL TRSLQHIDPH TAEYIERLSD ESDLYNNIVR TMLYQEEISK
     DESLTEPQRS LNRVVMRRLE HVYFKPSAVI KILDENCWKA IPAELDSTIT PRGSVQDAKT
     LVNILCNYLY INTEGEGLTK ARAMLCQIYF EALHDNYYKA RDMMLMSHLQ ETINSFDVHS
     QILFNRTLVQ VGLCAFRAGL VYEAQTTLQE ICGSGRQKEL LAQGVMIQRY NQVTPDQERL
     EKQRQLPFHM HINLELLECV YLTCSMLLEI PLFAQTGSSP DIKKRIISKT YRRMLEYHER
     QIFTGPPENT RDHVMQASKA LAQGEWKKAT DYIHSIKIWE LMSKPEEIKA MLSAQIQEEG
     LRTYLFTYAP YYDTLSVNRL SSMFELPDRK VAAIVSKMIS HEELAAALDQ VNSSIIFRKG
     VELSRLQSLA LSLSDKASGL IESNERTLET RTQGTANAFE RQGGRGGRGG NRGGRGGNRG
     GRGGISNAPR QAGGTQFTGG ALGAAVGSRA