ID A0A150VJI9_9PEZI Unreviewed; 741 AA.
AC A0A150VJI9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=M433DRAFT_56655 {ECO:0000313|EMBL:KYG50709.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG50709.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG50709.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG50709.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(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}.
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:KYG50709.1}.
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DR EMBL; JPDO01000001; KYG50709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VJI9; -.
DR STRING; 766039.A0A150VJI9; -.
DR Proteomes; UP000075602; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000075602};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03001}.
FT DOMAIN 39..126
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT COILED 635..662
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 741 AA; 85460 MW; 7A0CF7489E575F36 CRC64;
MAPSFEQLDP ETEYDDDEEI DYSDLREQYE VRMEEGLDTF IVIDGLPKVP PASKDKLVKF
LLRKLNTVGR TKEENVFMPM NDAGDMSEGF AFVEYETPAQ AAAAVKTLHA TPLDKKHTIA
VNKLTDIERY GREGRIDETY KPPEIPPFEE HEHLRWWLGD PEGRDQFVMF RGDNVGVFWN
NKDEAPEQVV DRMHWTESFV QWSPKGTYLT SMHTQGVQLW GGPNWSRQKR FMHPGVNLVD
FSPDERYLTT WSHRPMAVDE GHPVLSIEED GKNYIIWDIA TGKPLRSFVT LDLPGPTQDA
EGNPIKKKIQ WPAFKWSADA KYVARMNQGQ SISVYELPRM NLLDKQSIKI EGVMDFEWCP
ANPQRDNMKE YEQLFCYWTP EMGSNPAKVG LMSIPSKEIV RTRNLFNVSD AKLHWQSESA
FVCVKVDRHS KSKKSLATNL EIFRVREKGV PVEVVDSIKD TVINFAWEPK GDRFVLITAG
EVPAGSAVPP KTSVSFFCPE KAKGPAVGNF KLIRTVDKKN NNAIHWSPNG RFVVIATVLS
QQSFDLDFWD FDFEGEKDEK DKDLTANLQL MATADHYGVT DIEWDPSGRY VATSASVWKH
RMENGYHLYT FAGQLLREEP IEQFKQWAWR PRPERLLSKE EMKNVRKNLR EYSRQFEEAD
QAKKFSANKA VVDARRRMLE EWIAWRERVT AELLERRREL GLPDISEERA ALLAGESEDG
EGKVVEEIFE EILEESDEIL D
//
