ID A0A0B1SSH2_OESDE Unreviewed; 724 AA.
AC A0A0B1SSH2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=OESDEN_13777 {ECO:0000313|EMBL:KHJ86472.1};
OS Oesophagostomum dentatum (Nodular worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ86472.1, ECO:0000313|Proteomes:UP000053660};
RN [1] {ECO:0000313|EMBL:KHJ86472.1, ECO:0000313|Proteomes:UP000053660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ86472.1,
RC ECO:0000313|Proteomes:UP000053660};
RA Mitreva M.;
RT "Draft genome of the hookworm Oesophagostomum dentatum.";
RL Submitted (MAR-2014) 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; KN560320; KHJ86472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1SSH2; -.
DR Proteomes; UP000053660; 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 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; 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001, ECO:0000256|PIRNR:PIRNR036424};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03001};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03001}; Reference proteome {ECO:0000313|Proteomes:UP000053660};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}; WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT DOMAIN 70..122
FT /note="RRM"
FT /evidence="ECO:0000259|Pfam:PF00076"
FT DOMAIN 402..609
FT /note="Translation initiation factor beta propellor-like"
FT /evidence="ECO:0000259|Pfam:PF08662"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 83228 MW; F45ABDE8F122FF0B CRC64;
MVEMDVNKEN EEEPDFSDPE GYVDDISDEE LVMDVLRQQP SRDEYEEACL IIFGIPVVGP
ERIDKLRTVL SKVFKNVEPD HKAFFPLTEE GGSKGCVFIE FPDKVKAEYA KGVLNGYKLD
KNHVFSALLF NEARHFQKPQ ENWQPPKPTP YNDVGDLWWW MQHPRCRDQF AVQYEKDGVP
TVACYWHIKG HDPEIAGEAG KAERASWTDT VFKWSPHGSY LTTIHKRGVA LWGGPEFSRV
QRFAHDNVQF IDFSPCETYL VTYAEAAEKN HWGDDEDCLR IWDVVTGEML KGFSLYALTN
RDQLPCWPFF QWSFDEKFFA CLKAPEKDKL EKEKKVNGIS VFETETFKLV DHRNIIVDNI
KTFSWSPTAN IISYYAECTE SLPAEFGLVQ MPNQQRLRSG RIHNVAEAQM FWQKSGQRLA
VYTMRYSKKQ MKEGGEVKYV GGCTYHVEIF EIDKKDVSLM NLPLPEPFIN FGWEPYGDKF
CVLTGNQAKA TPLVYRIEPN SHAPKLISKL DAGVQFNEVS WAPAGGWLAV LAKRSTGGNV
MFVDTTLQEA KRTNVVEHPG FNKGYWDPTG RYFVTCSTLG GRMGADLGFR LYTFQGRELC
RKGLERLSQF KWRPRPPVKL SDQKLKEIKN NLKKTAVRFE REDNEEKNRA SQEVVEKRRK
IMAAFDVIRQ RNLKKIAAQK DLRISLRGGV DTDSMKADEL VEEQIMVALD TQKTLAPLGE
DELD
//
