ID A0A0N0RST2_9HYPO Unreviewed; 874 AA.
AC A0A0N0RST2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=ESCO_004636 {ECO:0000313|EMBL:KOS16753.1};
OS Escovopsis weberi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS16753.1, ECO:0000313|Proteomes:UP000053831};
RN [1] {ECO:0000313|EMBL:KOS16753.1, ECO:0000313|Proteomes:UP000053831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA Currie C., Gerardo N.M.;
RT "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT ant agriculture.";
RL Submitted (JUL-2015) 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}.
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:KOS16753.1}.
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DR EMBL; LGSR01000029; KOS16753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0RST2; -.
DR STRING; 150374.A0A0N0RST2; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000053831; 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; 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 {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:UP000053831}.
FT DOMAIN 615..789
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..58
FT /note="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 874 AA; 98509 MW; 3DE595C0AA98BCD0 CRC64;
MSRFFRRGGD DSSSESSSED EELYPDNEAE LSQEEESEEE DDSAFDNDSD EESDEGSEDG
EQKQGASRFL RDAASDSSDS DDEVRAKVKS AKLKRMDELD SSIKLIENGQ KIGDWSLISA
EFDKLNRQVA KLQDAGKTPK PYVKVLADLE DLMNDTIAKQ KVTPKKMNAI QARGLNAVKQ
KIKKIVKDYQ AQIQVYREDK DTYLWSSDEE EEVAPKAAKK TARFEETLVE DEAAAAAAAG
LDDGFATVGK GGRALQYTPE GIFKHLRSIM ETRGKKNTDR QEQIKVMEKL NEIANTPYQK
IRVLLGLVSA RFDLGSGTSN TMPLEHWKAA EKELSALLTT LGQEKEYVVL DNAEEWDDDE
KPPTLQPGEK YIKVSGSIVS YIERLDDELH RSLQSIDPHT SEYIDRLKDE GALYNIIFRG
LLYYENLKLD ETLDVPQESL NRIVMRRLEH IYFKPAQVVK TFEENCWKTV SEEAESSTTS
RTQAQEPATL VNVLCNYLYT HSDGIIRARA LLCQVYFLAL HDEYYKARDM MLMSHLQETV
NNFDVQSQIL YNRTLVQIGL CAFRQGLVYD AQNTLQEICG SGRQKELLAQ GFMMQRYNQV
SPEQERLEKQ RQLPFHMHIN LELLECVYLT CSMLLEIPLL AQTGSSPDVK KRVISKTYRR
MLEYHERQIF TGPPENTRDH VMQASKALAA GEWKKSTTFI NNIKIWDLMP NAEEIKTMLS
KQIQEEGLRT YLFTYAPFYD TLAIETLSGM FELDSTKVAA IISKMISHEE LAASLDQVTS
NVIFRKGVEL SRLQSLALTL SDKASALTEI NERTLEQRTQ GTSNAFERQG GRGRGGHRGG
ARGGRGGARG PGNAQRQAGG TQFTGGALGA AVRG
//
