ID A0A061DX04_THECC Unreviewed; 718 AA.
AC A0A061DX04;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=eIF-3-eta {ECO:0000256|HAMAP-Rule:MF_03001};
DE AltName: Full=eIF3 p110 {ECO:0000256|HAMAP-Rule:MF_03001};
GN ORFNames=TCM_006074 {ECO:0000313|EMBL:EOX96947.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX96947.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX96947.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(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; CM001880; EOX96947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061DX04; -.
DR STRING; 3641.A0A061DX04; -.
DR EnsemblPlants; EOX96947; EOX96947; TCM_006074.
DR Gramene; EOX96947; EOX96947; TCM_006074.
DR eggNOG; KOG2314; Eukaryota.
DR HOGENOM; CLU_011152_2_0_1; -.
DR InParanoid; A0A061DX04; -.
DR OMA; LWGGPQF; -.
DR Proteomes; UP000026915; Chromosome 2.
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; IBA:GO_Central.
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 GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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:UP000026915};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}.
FT DOMAIN 61..148
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 674..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 82814 MW; 2CCE5AED33AB71C3 CRC64;
MASEVMLMNE IESTAARLGI DLDNFDYSSV KLPPGEYCGI VSDDEDVYHD DQLEFDSGFG
NIIVVDNLPV VPREKFEKLE GVIRKIYSQI GVIKEDGLWM PVDPETKKTL GYCFIEYNTP
QEAELAKEKT NGYKLDRAHI FAVSMFDDFD KYMRVPDEWA PPEIKPYTPG ENLQKWLTDE
KARDQFVIRA GTDTEVLWND ARQSKTELVY KRAYWTESFV QWSPLGTYLA TVHRQGAAVW
GGANTFNRLM RYAHPQVKLI DFSPGEKYLV TYSSHEPSNP RDANRVVINI FDVRTGKVMR
DFKGSADEFA IGGTGGVAGV SWPVFRWGGG KEDKYFAKLG KNMISVYETE TFSLIDKKSL
KVENVVDFSW SPTDPIIALF VPELGGGNQP ARVSLVQIPS KEELRQKNLF SVSDCKMYWQ
SNGDYLAVKA DRYTKTKKST YTGFELFRIK ERDIPIEVLE LDNKNDKIIA FAWEPKGHRF
AVIHGDNPRP DVSFYSMRTA HNTGRVSKLT TLKGKQANAL FWSPGGRFIV LAGLKGFNGQ
LEFFNVDELE TMATAEHFMA TDIEWDPTGR YVATSVTSVH EMENGFNVWS FNGKLLYRIL
KDHFFQFLWR PRPPSFLTPE KEEEIARNLK KYSKKYEAED QDVSMLLSEQ DREKRRMLKE
EWDKWVSEWR RAHEEEKLER QKLRDGEASD EEEEYEAKEV EVEEVLDVSE EVLSYHEE
//
