ID A0A074ZQ46_9TREM Unreviewed; 674 AA.
AC A0A074ZQ46;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 03-MAY-2023, entry version 45.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
DE Short=eIF3b {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 9 {ECO:0000256|HAMAP-Rule:MF_03001};
GN ORFNames=T265_05147 {ECO:0000313|EMBL:KER27947.1};
OS Opisthorchis viverrini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX NCBI_TaxID=6198 {ECO:0000313|EMBL:KER27947.1, ECO:0000313|Proteomes:UP000054324};
RN [1] {ECO:0000313|EMBL:KER27947.1, ECO:0000313|Proteomes:UP000054324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT "Opisthorchis viverrini - life in the bile duct.";
RL Submitted (NOV-2013) 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}.
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DR EMBL; KL596711; KER27947.1; -; Genomic_DNA.
DR RefSeq; XP_009168335.1; XM_009170071.1.
DR AlphaFoldDB; A0A074ZQ46; -.
DR STRING; 6198.A0A074ZQ46; -.
DR GeneID; 20319329; -.
DR KEGG; ovi:T265_05147; -.
DR CTD; 20319329; -.
DR OrthoDB; 5479191at2759; -.
DR Proteomes; UP000054324; 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; 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:UP000054324};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}; WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT DOMAIN 31..115
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
SQ SEQUENCE 674 AA; 77758 MW; E76FDE0B54FE5E8D CRC64;
MPSFVDLVVD DNEIIADILA QKPEVEDHLG STIIVDGCPV VGPAKYDLLK KFLLEKFSKF
GTITEHDFPQ DEERQTKGYL FITYDNGKSA SQAVRAMNNT PLDKSHTFHV NLLAEYERLT
NVATEWKPPV KQPYKDFGNL KSWLLNEFCR DQFVVVHNDG EIGAVFWHNA VEPSLVEKRE
RWTDGWMRWS PRGTYLATMH QQGVILWGGE EFQRVGRFPH PGVKMIEFSP MENFMISLSP
SASAQMDEWD RPMADVIFWD VRRCMSRREF SIPIEAHPMF KWSHNDAYFA CLRDGCIVIY
ETNTFRLLDK KRLGGNIRDF SWSPAENILA YWVPESDNTP ARVVLMEVPS REELCTKNLF
SVAEIGLCWH EQGDFLAVQV LRCAKKKVDN EKQVKYVGTY MNLEIVRMRE KLYPVDQLGV
KASITCFQWE PHGTRFAFLQ TVASGKLSVA IYDVPRGSSI REVTVIEVPA ARNNELRWAP
RGGLLVVASL KSADGYLEFI SANEAQSLAK GDHPMVSEIH WDPTGRYLAT VVSSFYQKND
NGIWFWNCVG RCLFKMPLNG LRTFAWRPRP PCLLSSEQLQ ALKKNMQKYN NHFANEDRML
ASKASRELLE KRQRMVSEFN LWKNALIKQF NSEKQERMEL RGNENALDGE QQMEEELEFL
VSTVKEVLRK NTEE
//
