EIF3B_SCLS1
ID EIF3B_SCLS1 Reviewed; 744 AA.
AC A7EHM8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Eukaryotic translation initiation factor 3 90 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03001};
DE Short=eIF3 p90 {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Translation initiation factor eIF3, p90 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03001};
GN Name=prt1; ORFNames=SS1G_04820;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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:0000255|HAMAP-Rule:MF_03001}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC Rule:MF_03001}.
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DR EMBL; CH476625; EDO02344.1; -; Genomic_DNA.
DR RefSeq; XP_001595012.1; XM_001594962.1.
DR AlphaFoldDB; A7EHM8; -.
DR SMR; A7EHM8; -.
DR STRING; 665079.A7EHM8; -.
DR EnsemblFungi; EDO02344; EDO02344; SS1G_04820.
DR GeneID; 5490837; -.
DR KEGG; ssl:SS1G_04820; -.
DR VEuPathDB; FungiDB:sscle_02g013860; -.
DR eggNOG; KOG2314; Eukaryota.
DR HOGENOM; CLU_011152_4_0_1; -.
DR InParanoid; A7EHM8; -.
DR OMA; NVADCKI; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:EnsemblFungi.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:EnsemblFungi.
DR GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
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; 2.130.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 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; PTHR14068; 1.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF036424; eIF3b; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome;
KW Repeat; RNA-binding; WD repeat.
FT CHAIN 1..744
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000366879"
FT DOMAIN 40..126
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 193..232
FT /note="WD 1"
FT REPEAT 234..290
FT /note="WD 2"
FT REPEAT 307..348
FT /note="WD 3"
FT REPEAT 577..622
FT /note="WD 4"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 85249 MW; 0ECCB8159EC67EB6 CRC64;
MAPSFDHLPD PEEDEYDEEE LDISDLRERF EVQLEQGLDT FVVIDGLPEV NEDTKPKLIK
FLLRKLDSVG QTKKDSIHMP IGPDGKSFKF AFVEYSSPAE AIAACKALDG VPLDKKHTLR
VNKLTDIDRY GREGRIDENY TPPKIEEFTE KEHLRSWLAD PAGRGRDQFV MYKDDRVQVF
WNNEKDAPES IVDRQHWTES FVQWSPQGTF LTSMHQQGVQ LWGGPSWTRQ KRFAHPFVNL
VDFSPGEKYL TTWSNRPISI GEEGHPALSV DDDGKNYVIW DIETGLPLRS FANLDLPSNS
VDAEGNPVKR KIQWPAFKWS SDDKYVARLT QGSSISVYEL PRMNLLDKTS IKIDGVMDFD
WAPATPHREG VKNYEQLFCY WTPEIGSNPA KVGLMSIPSK EVVRTLNLFS VTDAKLHWQS
DASYLCVKVD RHSKSKKSLA TSLEIFRVKE KGVPVEVVDS IKDTVINFAW EPKGDRFVII
TTAEVVAATA VPPKTSVSFF CPEKVKGNGV GNFKHIRTYD KKNSNAIYWS PKGRFVIVAT
VHSQQSFDME FYDMDFEGEK PESDKDLTAN LQLMNTADHY GVTDIDWDPT GRFVATSASI
WKHTMENGYH LYDFKGEQLR EEPVEKFKQW LWRPRPPTLL SKEEQKQIRK NLREYSKVFD
QEDADRGASA DLAVVEHRRR LLDEWLAWRA NIEEDVQAER EDAGLPRDPL EPLKSKMASG
DEGQAIEIEE IVEEIVEETE EIIS
