ID F4X5V9_ACREC Unreviewed; 703 AA.
AC F4X5V9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=G5I_13750 {ECO:0000313|EMBL:EGI58199.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI58199.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) 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; GL888742; EGI58199.1; -; Genomic_DNA.
DR RefSeq; XP_011066137.1; XM_011067835.1.
DR AlphaFoldDB; F4X5V9; -.
DR STRING; 103372.F4X5V9; -.
DR EnsemblMetazoa; XM_011067835.1; XP_011066137.1; LOC105153154.
DR GeneID; 105153154; -.
DR KEGG; aec:105153154; -.
DR eggNOG; KOG2314; Eukaryota.
DR InParanoid; F4X5V9; -.
DR OrthoDB; 5479191at2759; -.
DR Proteomes; UP000007755; 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|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:UP000007755};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}; WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT DOMAIN 64..149
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 81558 MW; 38AD90E16FD8B2CA CRC64;
MAKKTQAEKT AQNDETAKGN DDPMNDDEEP NFSDPEGFVD DITDEELLGD ILKQKPSETD
GVESVIVVDN VPRVEPDKLE KLQSVINKVL GKFGTIVNQY YPMNETDGKT KGYIFLEYNN
HLNALTAVKS TNNYKIDKSH TFKVNLFTDF KKFEDIPENW EPPKAQPFKA ASDLHYHLLE
PDAYDQFCVL CGNGAGVSVQ IWQNSAPEPT LLEERNRWTE TYVKWSPLGT YLATFHKLGV
ALWGGPQFTQ QARFSQRGVE CIDFSPCERY LVTYTPRTDL GQDQKRLVIW DILSGQEKRS
FFPDGSSVWP IFRWSHDDKY LARMGEDILS VYETPSFGLL DKKSIKIPGI RDFSWSPTDN
VLAYWVPEDK DVPARVTLLE IPNRNEIRNK NLFNVADCKI FWQKSGDYLC VKVDRFAKRK
EKTEQKYTGM SYNFEIFHMR EKQIPVDSVE IKEPIHAFAW EPVGSKFAII HGEIPSVNVS
FYEVRYGHQP ALLKRLEKKA CNHLFWSPSG QFIVLAGLTT MAGALEFIDT NDFTIMNSTD
HYQTSDVEWD PTGRYVVTAV SSWKTSVDNG YWIWTFQGRI LKRVNLTAFN QLLWRPRPPT
LLTAEQIKEI KKNLKKYSAQ FESKDRMRLT RASKELIEKR CLLMKAFEEY RTKRIDEWNN
QKKRRLELRC NIDTDELDSD SKNVEEEVVE FFVKEETFVI DDK
//
