ID A0A2T3Z2R6_9HYPO Unreviewed; 749 AA.
AC A0A2T3Z2R6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000256|HAMAP-Rule:MF_03001};
DE Short=eIF3b {ECO:0000256|HAMAP-Rule:MF_03001};
DE AltName: Full=Eukaryotic translation initiation factor 3 90 kDa subunit homolog {ECO:0000256|HAMAP-Rule:MF_03001};
DE Short=eIF3 p90 {ECO:0000256|HAMAP-Rule:MF_03001};
DE AltName: Full=Translation initiation factor eIF3, p90 subunit homolog {ECO:0000256|HAMAP-Rule:MF_03001};
GN Name=PRT1 {ECO:0000256|HAMAP-Rule:MF_03001};
GN ORFNames=M441DRAFT_28279 {ECO:0000313|EMBL:PTB39111.1};
OS Trichoderma asperellum CBS 433.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB39111.1, ECO:0000313|Proteomes:UP000240493};
RN [1] {ECO:0000313|EMBL:PTB39111.1, ECO:0000313|Proteomes:UP000240493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB39111.1,
RC ECO:0000313|Proteomes:UP000240493};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-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 and, together
CC with other initiation factors, stimulates binding of mRNA and
CC methionyl-tRNAi to the 40S ribosome. {ECO:0000256|PIRNR:PIRNR036424}.
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S 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_03001}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03001,
CC ECO:0000256|PIRNR:PIRNR036424}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001,
CC ECO:0000256|PIRNR:PIRNR036424}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000256|HAMAP-
CC Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ679264; PTB39111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3Z2R6; -.
DR STRING; 1042311.A0A2T3Z2R6; -.
DR OrthoDB; 5479191at2759; -.
DR Proteomes; UP000240493; 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:UniProtKB-UniRule.
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; cd12278; RRM_eIF3B; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR HAMAP; MF_03001; eIF3b; 1.
DR InterPro; IPR011400; EIF3B.
DR InterPro; IPR034363; eIF3B_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR14068; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 EIF3 -RELATED; 1.
DR PANTHER; PTHR14068:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT B; 1.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF036424; eIF3b; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03001,
KW ECO:0000256|PIRNR:PIRNR036424};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03001,
KW ECO:0000256|PIRNR:PIRNR036424};
KW Reference proteome {ECO:0000313|Proteomes:UP000240493};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}.
FT DOMAIN 42..128
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 85477 MW; 90E94D483085AB1D CRC64;
MAPSFDQLRE ADLDDDEFNE DEIDISDLRE KFEVQLEQGY DTFVVIDGLP EVTEDQKPKL
VKFLLKKLNT VGKTKEELIY MPMGEDGKSQ RFAFVEYSSP AEAQAATRQL DGVPLDKKHT
LRVNKITDIE RYGREGRVDE KYVAPEIEEF TEKEHLRWWL KDPSGRGRDQ FVMYRGDSVG
VFWNNEKDQP ENIVDRQHWT EAFLQWSPLG TYLASVHQQG VQLWGGASWS RQARFAHPFV
NLVAFSPNEK YIVTWSNRPI SIPETGHPAL SIDDEGKNYV IWDIETAAPL RSFANLDAPK
GEEGKPQPKM QWPAFKWSAD DKYVARLTPG ASISVYELPR MNLLDKTSIK IEGVVDFDWA
PATPQREGVK TYEQLFTYWQ PGTGSNPAKV GLMSIPSKEI VRSLNLFNVS DAKLHWQSDA
AYLCVKVDRH SKSKKSQATT LEIFRVKEKG IPVEVVDTIK DTVINFAWEP KGDRFALITT
TEPVGPTAVP PKTSVSFFCP EKAKGPYAGN FKLLRTLDKK NSNAIYWSPK GRFVVIATIA
NQQSSDLDFY DVDFEGEKPE SAKDLTANLQ LMNTADHYGV TDVEWDPSGR FVATWASAWK
HAMENGYHIY DFKGEALREE PIEKFKQFQW RPRPPTMLSK DEQKQIRKNL REYSRVFEQE
DADRGASADL AVVEARRRVL DEWHAWRAEV EAEVAEEREV LGLPQDPHAA LLEAKTKEVE
ALDGASNEND RVIEEIVEDV LEESEEIVA
//