ID   EIF3C_NEUCR             Reviewed;         872 AA.
AC   Q7SBD4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=nip-1; ORFNames=NCU07831;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002238; EAA33716.1; -; Genomic_DNA.
DR   RefSeq; XP_962952.1; XM_957859.3.
DR   AlphaFoldDB; Q7SBD4; -.
DR   SMR; Q7SBD4; -.
DR   STRING; 367110.Q7SBD4; -.
DR   PaxDb; 5141-EFNCRP00000007471; -.
DR   EnsemblFungi; EAA33716; EAA33716; NCU07831.
DR   GeneID; 3879100; -.
DR   KEGG; ncr:NCU07831; -.
DR   VEuPathDB; FungiDB:NCU07831; -.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; Q7SBD4; -.
DR   OMA; FRCGLIK; -.
DR   OrthoDB; 5482362at2759; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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: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; 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   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..872
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000364287"
FT   DOMAIN          613..787
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          812..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..55
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..827
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   872 AA;  98399 MW;  38611B9B0CC93EA1 CRC64;
     MSRFFRGGDD SSTDSSSEEE EVYTSEEEEE KVQAEDESSS EEESDEEESD EESSSDEEEG
     TKKKGASRFL QSDDESEEEE EEQSDDEATT KVKSAKDKRF DELESTISQI QNGQKINDWS
     LIANEFDKLN RQVVKLQDGS KAPKSYIKAI ADLEDFMNET LAKQKVTPKK MNATNARGLN
     AVKQRIRKNN KEYQTQIDAY RKDADAFMES DDEVAAPKVV SKVRFEAPVV SAEQQEEDDK
     GFSTVDSRGK VVQYTPESIL KHLRAIIESR GKKNTDRLEQ IKVMETLNKV VPITPYQKIR
     VLQTLISARF DLGAGGAAQM PLDQWKAAER DLASLLEILE KEKDHVVVEG AEEWDDDDKL
     PTIPEGEKYL KVPGSVVSLI ERLDDELTRS LQAIDPHTSE YIDRLTDEGS LYNTIFRGLL
     YYEHLRKDAS LEVPQESLNR IIQRRLDHVY YKPAQVVKIL EENAWKQVSA EADSEITPRS
     QSGDAGKLIN ILSNYLFENS EGIIRARAML CQIYFLALHD EYYKSRDLML TSHLQETIAN
     FDIATQILYN RTLVQVGLCA FRKGLVYDAQ NTLQEICGSG RQKELLAQGV MIQRYSQVTP
     EQERLEKQRQ LPFHMHINLE LLECVYLTCS MLLEIPLLAQ TGSSPDVKKR IISKTYRRML
     EYHERQIFTG PPENTRDHVM QASKALAAGE WKKATDFIHS IKIWDLMPNT EGIKTMLAKQ
     IQEEGLRTYL FTYAPFYDTL AIATLSSMFE LDSRKVSAVV SKMISHEELA AALDQVTETV
     IFRKGVELSR LQSLALTLSD KASSLIETNE RTLEQKTQGS ANAFSRKDNR GGGQRGGGQR
     GGRGGARTGG NPQRQAGGTQ FTGGALGNAV RG
//