ID   EIF3J_NEMVE             Reviewed;         247 AA.
AC   A7RSH7;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
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   ORFNames=v1g240395;
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6;
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(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. {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; DS469534; EDO45638.1; -; Genomic_DNA.
DR   RefSeq; XP_001637701.1; XM_001637651.1.
DR   AlphaFoldDB; A7RSH7; -.
DR   SMR; A7RSH7; -.
DR   STRING; 45351.EDO45638; -.
DR   EnsemblMetazoa; EDO45638; EDO45638; NEMVEDRAFT_v1g240395.
DR   GeneID; 5517623; -.
DR   KEGG; nve:5517623; -.
DR   eggNOG; KOG4813; Eukaryota.
DR   HOGENOM; CLU_085806_2_1_1; -.
DR   InParanoid; A7RSH7; -.
DR   OMA; MDSWEDF; -.
DR   OrthoDB; 1565510at2759; -.
DR   PhylomeDB; A7RSH7; -.
DR   Proteomes; UP000001593; 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; IBA:GO_Central.
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   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..247
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   J"
FT                   /id="PRO_0000365144"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          43..108
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..46
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   247 AA;  28370 MW;  71A877E6A7B1ACF9 CRC64;
     MADWDDEKFE PGEVPADGVT DKWEGEDEDD DIKESWDDDD EDEKKEDEAK NTEAAAPKKK
     KTLKQILKEK EEQKLLEEKR KAEEKQKLEE EDKELTPEEQ MAEKLRRQKI VEESDLLVAM
     DTFGVGTQEE ASRTGLDSMI PSTKEEFTEY SKLLVEKLTK FETNPEYIPF LEATLREICV
     SLDPEDIKKL SSTLNMLQSE KLKAQKGKKA KSKATKKATL TGGAKMGRKD EMDYSYGDLG
     NEYDDFM