EIF3B_BOMMO
ID EIF3B_BOMMO Reviewed; 695 AA.
AC Q1HDZ5;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 9 {ECO:0000255|HAMAP-Rule:MF_03001};
GN Name=eIF3-S9 {ECO:0000255|HAMAP-Rule:MF_03001};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang L.-L., Chen K.-P., Yao Q., Hu Z.-G., Gao G.-T.;
RT "RNA binding proteins in Bombyx mori.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_03001}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC Rule:MF_03001}.
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DR EMBL; DQ497202; ABF55967.1; -; mRNA.
DR RefSeq; NP_001037602.1; NM_001044137.1.
DR AlphaFoldDB; Q1HDZ5; -.
DR SMR; Q1HDZ5; -.
DR STRING; 7091.BGIBMGA007114-TA; -.
DR PRIDE; Q1HDZ5; -.
DR GeneID; 733052; -.
DR KEGG; bmor:733052; -.
DR CTD; 733052; -.
DR eggNOG; KOG2314; Eukaryota.
DR HOGENOM; CLU_011152_1_0_1; -.
DR InParanoid; Q1HDZ5; -.
DR OrthoDB; 1194797at2759; -.
DR Proteomes; UP000005204; 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; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
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 GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR CDD; cd12278; RRM_eIF3B; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.30.70.330; -; 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; PTHR14068; 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; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW Repeat; RNA-binding; WD repeat.
FT CHAIN 1..695
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000363792"
FT DOMAIN 60..144
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 164..205
FT /note="WD 1"
FT REPEAT 295..335
FT /note="WD 2"
FT REPEAT 338..373
FT /note="WD 3"
FT REPEAT 444..486
FT /note="WD 4"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 80615 MW; D0B664285DDADEA6 CRC64;
MAKKKGDEKA NPAPQSDNEE QNFEEEPDFD DPEDFVEIPE EELLADILEQ KPKESDGYEN
VVVVDGCPQV GPERLEKLQS VINKIFSKFG KIVNEYYPTT ENGLTTGYIF LEYSNPQNAA
EAVKATNNCK LDKQHTFLVN LFTDFQKYSD IPKEWEPPAP QPFKVQSDLQ WYLMDPDAYD
QFLVGIGTGV ALQVWQNALP EPLLLQERPN WTETYAVWSP LGTYLATFHW RGVALWAGPK
FSQFQKFFHP EARFISFSPC ENYMVTFSPS GDRGDDKKWI IGDIRTGQEK RSFPPPDEYV
TWPIFRWSKD DRFFARIGAD VLSVYETPGF GLLDKKSIKI PGIRDFSWSP SDNTLAYWVA
EDKDVPARVT LLEIPNRTEV RSKNLFSVAD CKIHWQKSGD YLCVKVDRYS KVKKDKIDIK
YSGMYYNFEI FHMREKEIPV DSVEIKEPIQ AFAWEPVGSK FSIIHGDPAN ISISFYQVNT
GQAPTLLKKF ERKPFNHLFW SPSGQFIVLA NLGLTGGALE FLDTNDFTIM NVADHYQMSG
IEWDPTGRYV VTGVSSLKCK MDCGYYIWSF QGKILRRVMK EGFAQFHWRP RPPTLLSEKQ
QKEIKKNLKK YYSQFESKDR MRSSKASKEL VAKRTEQMKK FTEYRESKIQ EWNEQKPRRL
ELRDYVDTDG LDTDAVNTVE EVIEFFVKEE QTVIE