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Database: UniProt
Entry: A0A6H5IQA4_9HYME
LinkDB: A0A6H5IQA4_9HYME
Original site: A0A6H5IQA4_9HYME 
ID   A0A6H5IQA4_9HYME        Unreviewed;       689 AA.
AC   A0A6H5IQA4;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   24-JAN-2024, entry version 10.
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 subunit 8 {ECO:0000256|HAMAP-Rule:MF_03002};
GN   ORFNames=TBRA_LOCUS11376 {ECO:0000313|EMBL:CAB0039637.1};
OS   Trichogramma brassicae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC   Chalcidoidea; Trichogrammatidae; Trichogramma.
OX   NCBI_TaxID=86971 {ECO:0000313|EMBL:CAB0039637.1, ECO:0000313|Proteomes:UP000479190};
RN   [1] {ECO:0000313|EMBL:CAB0039637.1, ECO:0000313|Proteomes:UP000479190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ferguson B K.;
RL   Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CADCXV010000973; CAB0039637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6H5IQA4; -.
DR   Proteomes; UP000479190; 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   HAMAP; MF_03002; eIF3c; 1.
DR   InterPro; IPR027516; EIF3C.
DR   InterPro; IPR008905; EIF3C_N_dom.
DR   InterPro; IPR000717; PCI_dom.
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; 2.
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 {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:UP000479190}.
FT   DOMAIN          425..624
FT                   /note="PCI"
FT                   /evidence="ECO:0000259|PROSITE:PS50250"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  80533 MW;  0D805CEC271B9EC6 CRC64;
     MSRFFATGSD SESDTSSKEE QIQRAPAAAF TYSDDEEDTK RVVRSAKEKR YGEIKNAIKL
     IGNQKKIKDI NPMLNTFEDM TKAYSKAGPV ISSVENGKTP TFYLRALVEL DDFIKEVWKD
     TDGRKSMSKS NSKALSTLRQ KLRKYIKEKD FEKEIEAFRE NPPKDDDDDE EERVLHCLSL
     IITQRILERI PEMLTLLLST NDIILTKSIP EDEEEYEKSP FKLHGCVLTL AERLDEEFIK
     LLKECDPHSN EYVERQGTPS ELCRIYIRKI EHLYYKFDPI VLKQKDGEIS ADALTSVKVM
     DKMCKYIYSH DETDRLRTRA ILSHIYHHSI HDNWFKARDL FLMSNLQENI HHSDPATQIL
     YNRAVAHLGL CAFRHANIKD AHNCLLDLMM TGKVKELLAQ GLMPQRQHER SKEQEKIEKQ
     RQMPFHMHIN LEVLECVYLV SAMLIEIPYM AGKYLIAKNI SLGNIFLSYC ISFSAHEFDA
     RRRMISKTYY QQLRSSERQS LVGPPESMRE HVVAASKAMR NGNWAVCNNF IINEKMNGKV
     WDLFYQADKV RAMLTKLIKE EALRTYLFTY SHVYDSISMP TLALMFELER ATVHSIISKM
     IINEELMASL DEPSETVVMH RSEPSRLQSL ALQLTDKVNN FVDSNERIFE MKQGNFRNQG
     NFRERFNRQD WGGRQRRERN RNNDERNNY
//
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