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Database: UniProt
Entry: A0A1L7WEP3_9HELO
LinkDB: A0A1L7WEP3_9HELO
Original site: A0A1L7WEP3_9HELO 
ID   A0A1L7WEP3_9HELO        Unreviewed;       747 AA.
AC   A0A1L7WEP3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=PAC_01122 {ECO:0000313|EMBL:CZR51247.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR51247.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR51247.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR51247.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) 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}.
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DR   EMBL; FJOG01000001; CZR51247.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7WEP3; -.
DR   STRING; 576137.A0A1L7WEP3; -.
DR   OrthoDB; 5479191at2759; -.
DR   Proteomes; UP000184330; 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   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   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:UP000184330};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03001}.
FT   DOMAIN          41..127
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   747 AA;  85950 MW;  DB481D3BC025F4F3 CRC64;
     MAPSFDHLPD PEEDDYDEDE ELDFSDLRER FEVQLEQGLD AFVVVDGLPE VTAETKPKLI
     KFLRRKLEPV GKVREESIHM PLGEDGKSER FAFVEYSTAA EAIAACKQLD GVPLDKKHIL
     RVNKLTDIER FGREGRIDEH YTPPHIEEFK ENEHLRSYLA DPSGRGRDQF VMYKDDRVQV
     FWNNEKDAPE SIVDRQHWTE SFVQWSPQGT YLTSMHQQGV QLWGGPSWTR QKRFAHPFVN
     LVDFSPGEKY LTTWSNRPIV IGEEGHPALS VDDDGKNYVI WDIETGKPLR SFANIELPSN
     SNDENGQPVK RKITWPAFKW SADDQYVARL TQGASISVYE LPRMGLLDKT SIKIDGVMDF
     DWAPATPHRD GVKTYEQLFC FWTPEMGSNP AKVGLMSIPS KEIVRTLNLF SVTDAKLHWQ
     SNADYLCVKV DRHSKSKKSL ATSLEIFRVK EKGVPVEVVD SIKDTVINFA WEPKGDRFVI
     ITTAEVVTPS AVPPKTSVAF YCPEKVKGAG VGNFRHIRTY DKKNSNAIYW SPKGRFVIVA
     TVHSQQSFDM EFFDMDFEGE KPESDKDLTA NLQLMNTADH YGVTDIDWDP TGRFVATSAS
     IWKHAMENGY HLYDFKGEQL REEPVEKFKQ WLWRPRPPTL LTKEEQKQIR KNLREYSKVF
     EQEDADRGAS ADLAVVEHRR RLLMEWLAWR EEIEHDVAEE RQELGMPLDP LEGLIKKTAT
     EADGEEEVIE IEELVEEIVE ETEEIVS
//
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