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Database: UniProt
Entry: A0A0D8Y3P1_DICVI
LinkDB: A0A0D8Y3P1_DICVI
Original site: A0A0D8Y3P1_DICVI 
ID   A0A0D8Y3P1_DICVI        Unreviewed;       719 AA.
AC   A0A0D8Y3P1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=DICVIV_03032 {ECO:0000313|EMBL:KJH50787.1};
OS   Dictyocaulus viviparus (Bovine lungworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae; Dictyocaulus.
OX   NCBI_TaxID=29172 {ECO:0000313|EMBL:KJH50787.1, ECO:0000313|Proteomes:UP000053766};
RN   [1] {ECO:0000313|EMBL:KJH50787.1, ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|EMBL:KJH50787.1,
RC   ECO:0000313|Proteomes:UP000053766};
RA   Mitreva M.;
RT   "Draft genome of the bovine lungworm Dictyocaulus viviparus.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HannoverDv2000 {ECO:0000313|Proteomes:UP000053766};
RX   PubMed=26856411; DOI=10.1038/srep20316;
RA   McNulty S.N., Strube C., Rosa B.A., Martin J.C., Tyagi R., Choi Y.J.,
RA   Wang Q., Hallsworth Pepin K., Zhang X., Ozersky P., Wilson R.K.,
RA   Sternberg P.W., Gasser R.B., Mitreva M.;
RT   "Dictyocaulus viviparus genome, variome and transcriptome elucidate
RT   lungworm biology and support future intervention.";
RL   Sci. Rep. 6:20316-20316(2016).
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; KN716197; KJH50787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D8Y3P1; -.
DR   STRING; 29172.A0A0D8Y3P1; -.
DR   Proteomes; UP000053766; 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; 1.
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   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:UP000053766};
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..604
FT                   /note="Translation initiation factor beta propellor-like"
FT                   /evidence="ECO:0000259|Pfam:PF08662"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   719 AA;  82500 MW;  D945A51B9AFDA39E CRC64;
     MVEIDGNKEN EEEPSFSDPE DYVDDVADEE LVMDVLRQHP SMDEYEESCL IIFGLPVVGA
     ERVPKLQTVL SKVFTNVEPQ HKAHFPLTAE GGSKGCVFIE FPDKARAEYA KGVLNGYKLD
     KNHVFSALLF NEARQFQKPP DDWQAPKPTP YNDVGDLWWW MQHPRCRDQF AVQYEKDGVP
     TVACYWHIKG HEPEIAGDSG KAERPSWTDT VFKWSPHGSY LTTIHKRGVA LWGGPEFARV
     QRFAHDNVQF IDFSPCETYL VTYAEAGEKN HWGDDDDCLR IWDAVTGEML KGFSLYALTN
     RDQLPCWPFF QWSFDEKYFA CLKPPEKDKL EKEKKVNGIS VFETEKFALV DHRNVIVENI
     KTFSWCPTQN IISYYAECTD SLPAEFGLVQ MPAQQRLRSG RIHNVADAQM FWQKSGQRLA
     VYTMRYSKKQ MKEGGEVKYI GGCTYHLEIF EIDKKDVSLM NLPLPEPFIN FGWQPYGEKF
     CVLTGNQAKV TPLVYRLEPN SHAPKLMSKL DPGVSWAPAG GWLAILAKRS NGGNVMFVDT
     TLQEAKRTNV VEHPGFNKSY WDPTGRYFVT CSTLGGRIGA DLGFRLYTFQ GRELCRKALE
     RLSQFKWRPR PPVKLSDQKL KEIKNNLKKT AVRFEREDNE EKNRASQEVV EKRRKIMAAF
     EMIRQKNLKK IAAERDIRIS LRDGVDTDSM KADELVEEQI MVALDTQKTL APLGEDELG
//
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