ID   EIF3C_CHAGB             Reviewed;         863 AA.
AC   Q2H731;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=CHGG_05534;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408031; EAQ88915.1; -; Genomic_DNA.
DR   RefSeq; XP_001221629.1; XM_001221628.1.
DR   AlphaFoldDB; Q2H731; -.
DR   SMR; Q2H731; -.
DR   STRING; 38033.XP_001221629.1; -.
DR   PRIDE; Q2H731; -.
DR   EnsemblFungi; EAQ88915; EAQ88915; CHGG_05534.
DR   GeneID; 4391333; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_2_1; -.
DR   InParanoid; Q2H731; -.
DR   OMA; VVMHRSE; -.
DR   OrthoDB; 273138at2759; -.
DR   Proteomes; UP000001056; 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:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
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; -; 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..863
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000364280"
FT   DOMAIN          604..778
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          808..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..51
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  97115 MW;  8016585D0C157EEA CRC64;
     MSRFFRGGDD SSSESSSDEE ELYSTSEEEE EEDQDQEESS EEEDEEESSD EDEGPKKTGL
     SRFLVDQASS DSEGSDEEGA TKVKSAKDKR FDELEATITT IQNRQKIDDW GSIANEFDKL
     NRQVVKLQDG GKAPKSYIKC IAELEDFLNE TLAKQKVTPK NKKLNATNAR GLNAVKQRIK
     KNNKDYQAQI DAFRKDSDDF MESDEEEVPA PKTKVRFQEA AAPEEAAEDE DKGFARVDKR
     GKAIPFSPES IQKHLRAIVE SRGRKNTDRG EQIKIMEELN KVAETPYLKI RVLQTLVSAR
     FDLGSGTTTS MPLDHWKAAE RELAALLTLL ETHKDHVVIE GAEEWEDDDK TPILGPDDKY
     IKVPGSVVSY IERLDDELTR SLQSIDPHTS EYIERLTDEA SLYNIILQGL LYYETIRKDA
     SLEIPQESLN RIIQRRLDHV YFKPAQVVKI LEENAWKQVS SGVDSAITPR GASGDAGKLM
     YTLCNYLFDN SEGIIRARAM LSQIYFLALH DEYYKARDMM LTSHLQESIA NFDVATQILY
     NRTLVQVGLC AFRRGLVYDA QNTLQDICGS GRQKELLAQG VMMQRYNQVT PEQERLEKQR
     QLPFHMHINL ELLECVYLTC SMLLEIPLLA QIGSSPDIKK RVISKTYRRM LEYHERQIFT
     GPPENTRDHV MQASKALAAG EWKKATHFIH SIKIWDLMPS SEEIKAMLAK QIQEEGLRTY
     LFTYAPFYDT LAIETLSTMF ELDSVKVSAV VSKMISHEEL AAALDQVTKT VIFRKGVELS
     RLQSLALALS DKASALIETN ERTLEVRTQG SANAFSRKDG RQGGQRGGGQ RSGRGGARAG
     GNAQRQAGGT QFTGGALGAA VRG