ID M7SLV9_EUTLA Unreviewed; 744 AA.
AC M7SLV9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=UCREL1_5614 {ECO:0000313|EMBL:EMR67374.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR67374.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(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; KB706451; EMR67374.1; -; Genomic_DNA.
DR RefSeq; XP_007793521.1; XM_007795330.1.
DR AlphaFoldDB; M7SLV9; -.
DR STRING; 1287681.M7SLV9; -.
DR KEGG; ela:UCREL1_5614; -.
DR eggNOG; KOG2314; Eukaryota.
DR HOGENOM; CLU_011152_4_0_1; -.
DR OMA; LWGGPQF; -.
DR OrthoDB; 5479191at2759; -.
DR Proteomes; UP000012174; 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 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; 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; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 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:UP000012174};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}.
FT DOMAIN 42..128
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 699..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 85995 MW; C2BD819D89740370 CRC64;
MAPSFDHLRD ADIDEDDYDE DEIDFSDLRE KYEVQLEQGY DTFVVVDGLP QVTEEQKPKL
VKFLLKKLNT VGRTREDLIY MPMGEDDKSL RFAFVEYSSA AEAAAAVRQL DMVPLDKRHT
IRVNKMTDID RYGREGRVDE EYTAPKIEPF QEKEHLRSFL ADPSGRGRDQ FAMFRGDNVG
VFWNNEKDTP ENIVDRQHWT ESFVQWSPLG TYLVSVHQQG VQLWGGQSWS RQRRFAHPFV
NMLDFSPSER YVVTWSNRPI SIPDEGHPQL SMDEDGKNYV IWDLETSKPL RSFANLDIPS
SNDPNAPPKP APKFPWPAFK WSSDDRYVAR LNQGQSISVY ELPRMNLLDK MAIKLEGVMD
FEWAPATPQR DGVKLYEQLF CFWTPEIGSS PARVGLMSMP SKQVVRSLNL FSVSDAKLHW
QSDAAYLAVK VDRHSKSKKS QATTLEIFRV KEKGVPVEVV DTIKDTVINF AWEPKGDRFV
VITTTEPIGP TAVPPKTSVA FFCPEKAKGS VIGNFRHLRT LEKKNSNSIY WSPKGRFVVV
ATIANQQSSD LDFFDLDFEG EKPESDKDLT ANLQLMNVAD HYGVTDLQWD PSGRFVASWA
SVWKHTMENG YHLYDFRGEQ LREEPVDKFK QWLWRPRPAT LLTKDEQKQI RKNLREYSRQ
FEQEDAERGA SADLAVIEAR RRILDEWYAW RASVEEELEE EREFRGLPKK PLEEEQAAEA
DEGEKQVIEE IVEEVLEEHE EIVP
//
