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EIF3J_DROVI
ID   EIF3J_DROVI             Reviewed;         236 AA.
AC   B4LN42;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit J {ECO:0000255|HAMAP-Rule:MF_03009};
DE            Short=eIF3j {ECO:0000255|HAMAP-Rule:MF_03009};
GN   Name=eIF3j {ECO:0000255|HAMAP-Rule:MF_03009};
GN   Synonyms=Adam {ECO:0000255|HAMAP-Rule:MF_03009}; ORFNames=GJ21266;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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_03009}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. The eIF-3 complex interacts with pix.
CC       {ECO:0000255|HAMAP-Rule:MF_03009}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit J family. {ECO:0000255|HAMAP-
CC       Rule:MF_03009}.
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DR   EMBL; CH940648; EDW60046.1; -; Genomic_DNA.
DR   RefSeq; XP_002048853.1; XM_002048817.2.
DR   AlphaFoldDB; B4LN42; -.
DR   SMR; B4LN42; -.
DR   STRING; 7244.FBpp0235683; -.
DR   EnsemblMetazoa; FBtr0237191; FBpp0235683; FBgn0208399.
DR   GeneID; 6626063; -.
DR   KEGG; dvi:6626063; -.
DR   eggNOG; KOG4813; Eukaryota.
DR   HOGENOM; CLU_085806_2_0_1; -.
DR   InParanoid; B4LN42; -.
DR   OMA; HYGLFLE; -.
DR   OrthoDB; 1565510at2759; -.
DR   PhylomeDB; B4LN42; -.
DR   ChiTaRS; Adam; fly.
DR   Proteomes; UP000008792; 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:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006446; P:regulation of translational initiation; IEA:EnsemblMetazoa.
DR   Gene3D; 1.10.246.60; -; 1.
DR   HAMAP; MF_03009; eIF3j; 1.
DR   InterPro; IPR023194; eIF3-like_dom_sf.
DR   InterPro; IPR013906; eIF3j.
DR   PANTHER; PTHR21681; PTHR21681; 1.
DR   Pfam; PF08597; eIF3_subunit; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..236
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   J"
FT                   /id="PRO_0000365141"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          61..112
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT   COILED          174..209
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT   COMPBIAS        27..42
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..230
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   236 AA;  27024 MW;  C4D448E976C83081 CRC64;
     MADDWESAAD SEIVIRPNAT NNINKWEGED DDEDVKESWE DEEEKKDEEK PTKTEAPVKT
     KPNKALKAKL EEQERLNEEE ERKRLANMTA EEKLAEKLRL QKIQEESDLK SALDTFGVTS
     IGGGLDAFNP QSKEEFKEFG ATLSWKVAQY RESVHFPEFI EDLVRSLCVN LSAADIKKVK
     MSVESLHSEK QKMEKANAKK SAAKAKGKVS LRKESDDIDD YQKYGNDFTD DYDDFM
 
 
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