EIF3F_ASPTN
ID EIF3F_ASPTN Reviewed; 345 AA.
AC Q0CCM5;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit F {ECO:0000255|HAMAP-Rule:MF_03005};
DE Short=eIF3f {ECO:0000255|HAMAP-Rule:MF_03005};
GN ORFNames=ATEG_08559;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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:0000255|HAMAP-Rule:MF_03005}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit F family. {ECO:0000255|HAMAP-
CC Rule:MF_03005}.
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DR EMBL; CH476606; EAU30691.1; -; Genomic_DNA.
DR RefSeq; XP_001217145.1; XM_001217144.1.
DR AlphaFoldDB; Q0CCM5; -.
DR SMR; Q0CCM5; -.
DR STRING; 341663.Q0CCM5; -.
DR EnsemblFungi; EAU30691; EAU30691; ATEG_08559.
DR GeneID; 4323278; -.
DR VEuPathDB; FungiDB:ATEG_08559; -.
DR eggNOG; KOG2975; Eukaryota.
DR HOGENOM; CLU_027018_0_0_1; -.
DR OMA; MADTDSF; -.
DR OrthoDB; 1038775at2759; -.
DR Proteomes; UP000007963; 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: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:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; 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 CDD; cd08064; MPN_eIF3f; 1.
DR HAMAP; MF_03005; eIF3f; 1.
DR InterPro; IPR027531; eIF3f.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR PANTHER; PTHR10540:SF6; PTHR10540:SF6; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..345
FT /note="Eukaryotic translation initiation factor 3 subunit
FT F"
FT /id="PRO_0000364326"
FT DOMAIN 30..166
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 308..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 37156 MW; 46561CE947710BD3 CRC64;
MAAADPFLHL ARPLGPVAVG SAPTTAPLNV VIQPQALFSI LDHSLRRNAD QERVIGTLLG
TRSEDGTEVE IRSTFAVGHT ETTDQVEVDM EYQKQMLALH LKANPKEVLV GWYATSSELN
TFSALIQNFY SGQGDGTFPH PAVHLTVSTE PGKDIETRAY ISAPVGVTAE RAADSAAFIP
VPHEIRYGET EKSGLEAIAA ARDAEERAAN LFTDIEALER AIEEVLGMID RVSRYVESVI
DEEAPASTAL GQFLLNALAL APKVEPADIE RDFNNHIQDV LVVSYLANTI RTQMELSNRL
ATAQLTLGGE SGSTESGQRG GQRGGKGGRG GQQRNQERSG EEVRA