EIF3J_ASPCL
ID EIF3J_ASPCL Reviewed; 268 AA.
AC A1CE66;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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};
DE AltName: Full=Eukaryotic translation initiation factor 3 30 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03009};
DE Short=eIF-3 30 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03009};
GN Name=hcr1; ORFNames=ACLA_088540;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027052; EAW11165.1; -; Genomic_DNA.
DR RefSeq; XP_001272591.1; XM_001272590.1.
DR AlphaFoldDB; A1CE66; -.
DR SMR; A1CE66; -.
DR STRING; 5057.CADACLAP00008140; -.
DR EnsemblFungi; EAW11165; EAW11165; ACLA_088540.
DR GeneID; 4705000; -.
DR KEGG; act:ACLA_088540; -.
DR VEuPathDB; FungiDB:ACLA_088540; -.
DR eggNOG; KOG4813; Eukaryota.
DR HOGENOM; CLU_087988_0_0_1; -.
DR OMA; HYGLFLE; -.
DR OrthoDB; 1484669at2759; -.
DR Proteomes; UP000006701; 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 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..268
FT /note="Eukaryotic translation initiation factor 3 subunit
FT J"
FT /id="PRO_0000366905"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 40..95
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 268 AA; 30062 MW; 02F5C56442D42F9E CRC64;
MTPSKWDDEE ESVSPPPVVN RRKFDDEEDE EVLDSWDAAE DSEVEREKAA KAAEAKAKAE
AEAAAKKKSK AQRIEEHKAE RRKNAEADSE EDEDEDEDEA EKRARLRRTE KDSDLKHAED
LFGDIDLNRS RNRGAPKAIV ISDSADPTQA VDLSAMPLFK PTTKDQFARL TTTLIPLLTA
HSKKPHYALW AQEFTKQLVK ELNSGDVKKI ASALTTVSNE KMREERAADK GSKKSKAAKT
KVSLVANRDN KIDATSYDDD GLEDDDFM
