ID A0A319A1Q0_ASPLB Unreviewed; 865 AA.
AC A0A319A1Q0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=BO96DRAFT_458710 {ECO:0000313|EMBL:PYH53746.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH53746.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH53746.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH53746.1,
RC ECO:0000313|Proteomes:UP000247441};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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; KZ821361; PYH53746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319A1Q0; -.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000247441; 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}.
FT DOMAIN 603..777
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..865
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"
SQ SEQUENCE 865 AA; 97777 MW; 7463DAEA69F3EA9C CRC64;
MSRFFYGGGS DSESSSSEEE ELYSDREEEE QSEEESSEEE SEEEEESSSE DEDAGKTGAN
RFMKNVSESD ESEDEERVTI VKSAKDKRLE ELENTVKLIE NAEKISDWAV ISTEFDKLNR
QIVKIVQSGP TPKIYVKTVA DLEDFVNETI SKQKSSNKKM NASNAKGFNA VKQRIKKNNK
DYAVQIDKYR KDKDGFMEAK EEVARPVAAA PRLTKIERIE APALSTAGDD DGFATVGRGG
KTLQYTPESI LKHLRVIVES RGKKNTDRLE QIRTMEKLLE VAQTPYQRIR IYLTMISTRF
DLTSSSTSNY MAVDQWKFAE QEFATLLSVL ENNRTYVVTE GAEEWEDDEK QPTPAPGEVV
HIPGSIVSYV ERLDDELTRS LQHIDPHTAE YIDRLGDEKQ LYANLVRTQV YVEGLTQSEK
TDPRQDSLNR VVMRRLEHIY FKPSQVVTIL EEGTWKVLPS ELESNVTPRG NTGDVTNLVQ
TLCSYLFKHS DGIIRARAML CQIYFLALHD QYYRSRDLML MSHLTENIAN FDVSTQILFN
RTLVQIGLCA FRAGLIYEAQ TTLSEVCGSG RQKELLAQGI ILQRYSTVSP EQERLERQRQ
LPFHMHINLE LLECIYLTSS MFLEVPLMAQ TSSSPEMKRR VISKTFRRML DYNERQVFTG
PAENTRDGVI MSAKFLAAGD WKKAAEMLNS IKIWDLMPQP DKVKEMLSQQ IQEEGLRTYL
FTYAPFYDSL SISTLATMFE LPEKKIAAII SRMISHEELA AALDQVNDAI VFRKGVELSR
LQSQIVTLAD KSMNLLESNE KTLEQRTQGM ANAFQRDQGA GARGGRGPRG GGQARGGPRF
PGGQQGRRPG GQQFSGGALG GAIKA
//
