ID A0A0M0JCG0_9EUKA Unreviewed; 580 AA.
AC A0A0M0JCG0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 subunit 9 {ECO:0000256|HAMAP-Rule:MF_03001};
GN ORFNames=Ctob_003560 {ECO:0000313|EMBL:KOO24037.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO24037.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000256|HAMAP-
CC Rule:MF_03001}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOO24037.1}.
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DR EMBL; JWZX01003133; KOO24037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0JCG0; -.
DR OrthoDB; 5479191at2759; -.
DR Proteomes; UP000037460; 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; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR HAMAP; MF_03001; eIF3b; 1.
DR InterPro; IPR011400; EIF3B.
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 SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03001,
KW ECO:0000313|EMBL:KOO24037.1};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03001};
KW Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}.
FT DOMAIN 262..463
FT /note="Translation initiation factor beta propellor-like"
FT /evidence="ECO:0000259|Pfam:PF08662"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..580
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 67251 MW; 3CEB87DB4B6F46A7 CRC64;
MATSLTNRTR SSRARSRTTP STWPCPTRSE SLRHRPSCPR RICTSGSRTA KARDQYVCRY
NEMTEIWWND PQKPNQEPSY SKKNWSDTYV TWSPRGTYLA TFHRLGIMLW GGPSWKRQIK
INHGGVKLID FSPCETYLVT WSPESGQSAA LIIWEIKTGN KCRALQGSDP ASEMRWPAYL
WSHDDSLFAR LGDDCIYVYE SSTMKLIKDK QDKRTSVRVE GVRQFLWSPT DNIISCWIPE
HTNNPAKVVL MSLPSREELR QKNLFSVADL RMTWHDQGHF LCVKVDKHSK SKKTLNSAFE
LFRLRDKDVP IEVTEFTKET TVIAFAWEPK GIRYAIIHGE AGSQRTDVSF YSMGSKYNGR
ISLIKTLESK TCSTLWWSPV GSIIVLANLK GTAGQLEWVD ANTQTTIGEA EHFMCSDVEW
DPTGRFVATS VSHWKHQMEN GFIMWSSHGR ELLHTKHDKF YQLHWRPRPK TLLTEAQEKE
IRKNLRKYSH RYEEEDAQLK NQLGADKLRE RKEKHAAFEG FLRAKQKEYD DMRARRIELR
GGVESDAESA YTLIEEEERE QLEMTEEVLD AGEEIEIGDD
//
