ID S7ZH11_PENO1 Unreviewed; 742 AA.
AC S7ZH11;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=PDE_04524 {ECO:0000313|EMBL:EPS29574.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS29574.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS29574.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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}.
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DR EMBL; KB644412; EPS29574.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZH11; -.
DR STRING; 933388.S7ZH11; -.
DR eggNOG; KOG2314; Eukaryota.
DR HOGENOM; CLU_011152_4_0_1; -.
DR OrthoDB; 5479191at2759; -.
DR PhylomeDB; S7ZH11; -.
DR Proteomes; UP000019376; 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; 2.
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 SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 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:UP000019376};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}.
FT DOMAIN 40..126
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 84674 MW; F370C6B019F04CD8 CRC64;
MAPSFDTLSE QDFHEEEEEE IDFSDLKEQF EVKMEEGLDT FVVVDGLPVV PEDSRQKLVK
FLLRKLNTVG HTSEDAVFMP LNDKGMSEGF AFVEFETPEQ ALAAVKQLHG VPLDKKHTLA
VNKLMDIERY GREGRIEEEY HAPELEPFKE KEHLRSWMAD ANARDQFALY RGDKVGVFWN
NKSNPPENVV DRAHWTQLFV QWSPKGTFLA SVHPQGVQLW GGASFSKQKQ FPHPFVQLVE
FSPLEGYLTT WSSRPIQVEE GQPILTFEED GKNIIVWDIE SGKPLRSFVS HDLAGGPAVE
GDVQPKKKVQ WPAFKWSADE KYVARMLQGQ SISIYEVPNM NLLGRTSVKV EGVNDFEWSP
ATVTREGVKQ YEQLLCFWTP EIGSNPARVA MMSVPSKEIV RTRNLFNVSD VKLHWQSQGA
YVCVKVDRHS KSKKSMATNL EIFRVREKGV PVEVVDSLKD TVINFSWEPN GSRFVVITNG
EAPTGAAVLP KTAVSFFAPE KKGNTTGNFK LVRTIEKKTS NGIYWSPKGR FVVVATVHSQ
TNFDLDFWDM DFEGEKNEAE KDLAANLQLM KTNEHYGVTD IEWDPTGRYV VSSASVWTHS
MENGWNLHTF AGQTLSENPT EKFKQFLWRP RPPTLLSKEE QKQVRKNLRE YSKEFDEEDR
FAVDIANTAV VEQRKRVLSE WLAWMRREKE IQAEEREAFG LPEDADSPKR AKDAVAVNQQ
EGDTVVEEIV EEIVEETEEV IG
//
