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Database: UniProt
Entry: A0A066W551_TILAU
LinkDB: A0A066W551_TILAU
Original site: A0A066W551_TILAU 
ID   A0A066W551_TILAU        Unreviewed;       757 AA.
AC   A0A066W551;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
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 90 kDa subunit homolog {ECO:0000256|HAMAP-Rule:MF_03001};
DE            Short=eIF3 p90 {ECO:0000256|HAMAP-Rule:MF_03001};
DE   AltName: Full=Translation initiation factor eIF3, p90 subunit homolog {ECO:0000256|HAMAP-Rule:MF_03001};
GN   Name=PRT1 {ECO:0000256|HAMAP-Rule:MF_03001};
GN   ORFNames=K437DRAFT_246841 {ECO:0000313|EMBL:KDN45875.1};
OS   Tilletiaria anomala (strain ATCC 24038 / CBS 436.72 / UBC 951).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Georgefischeriales; Tilletiariaceae; Tilletiaria.
OX   NCBI_TaxID=1037660 {ECO:0000313|EMBL:KDN45875.1, ECO:0000313|Proteomes:UP000027361};
RN   [1] {ECO:0000313|EMBL:KDN45875.1, ECO:0000313|Proteomes:UP000027361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UBC 951 {ECO:0000313|EMBL:KDN45875.1,
RC   ECO:0000313|Proteomes:UP000027361};
RG   DOE Joint Genome Institute;
RA   Toome M., Kuo A., Henrissat B., Lipzen A., Tritt A., Yoshinaga Y., Zane M.,
RA   Barry K., Grigoriev I.V., Spatafora J.W., Aimea M.C.;
RT   "Draft genome sequence of a rare smut relative, Tilletiaria anomala UBC
RT   951.";
RL   Submitted (MAY-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}.
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:KDN45875.1}.
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DR   EMBL; JMSN01000039; KDN45875.1; -; Genomic_DNA.
DR   RefSeq; XP_013243313.1; XM_013387859.1.
DR   AlphaFoldDB; A0A066W551; -.
DR   STRING; 1037660.A0A066W551; -.
DR   GeneID; 25263233; -.
DR   HOGENOM; CLU_011152_4_0_1; -.
DR   InParanoid; A0A066W551; -.
DR   OMA; LWGGPQF; -.
DR   OrthoDB; 5479191at2759; -.
DR   Proteomes; UP000027361; 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   PIRSF; PIRSF036424; eIF3b; 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:UP000027361};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03001}.
FT   DOMAIN          41..129
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
SQ   SEQUENCE   757 AA;  86733 MW;  1D6472CC57B9CC36 CRC64;
     MNGSAATTSN ATLEDQFEDL EIDYSDIEAK YAVDVHETLD DVIVIDGVPS VGKDREAKLL
     ETVAKRFKQY AGLDVNIASM QLPYDDDGKS KGYMFIEMNS AQDATTAIKL MDQYPFDKKH
     RFFVNRFTDI EKLANLDETY SEPAIEAFKE KEHLRSWLAD SRGRDQLVMC QNESVSVHWH
     QRTGSPQEIQ KRERWTESYV SWSPLGTLLA TFRIQGVTLW GGPAFSLYQR FAHPGVRLID
     FSPNEKYIVT WSPQPIVVPE NMPQGPQYFA PQDEGNRVAV WDVGTGHLLR TFPVSPDEGS
     NAGGSGAKGF TWPFLKWSGD DMYCARIVPG KKISVFQLPT MGLLEKKSIE IEGVVDFEWC
     PLGDKDKDAI EAYENAVKEA KEGKVAVKKP KDNMLVFWVP EVANQPARVS VMSIPTREIL
     RTKNLFNVSD CKLHWHPQGD YLCVKVDRHT KTKKSMFCNL ELFKMREKNL PVEVIELKDP
     VTAFAWEPQG SHFALISSND PNLGAAAPGI TIKTQINLYY YDTKKGDFRS LKVLDNKTSN
     TLYWSPKGRH LVVATMGSSQ KFDLEWYDVD LGYEQRQGQP ANDPAEEVKQ IGAGEHYGIT
     DLEWDPSGRY VITSASVWRH TMENGYAIWD WRGNELQKHV LERFKQILWR PRPRTLLSKE
     QQKAVRRNVR EIGKQFEEED AAEESNAALQ HRELYQRKLD EWKAWRQANL AELNERRVDA
     GLEPVVTVHE QLQQQHVEES QEWIEEVLEE TTEEVVE
//
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