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Database: UniProt
Entry: E4UZL3_ARTGP
LinkDB: E4UZL3_ARTGP
Original site: E4UZL3_ARTGP 
ID   E4UZL3_ARTGP            Unreviewed;       745 AA.
AC   E4UZL3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=MGYG_06539 {ECO:0000313|EMBL:EFR03543.1};
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN   [1] {ECO:0000313|Proteomes:UP000002669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS989826; EFR03543.1; -; Genomic_DNA.
DR   RefSeq; XP_003171997.1; XM_003171949.1.
DR   AlphaFoldDB; E4UZL3; -.
DR   STRING; 535722.E4UZL3; -.
DR   GeneID; 10027257; -.
DR   VEuPathDB; FungiDB:MGYG_06539; -.
DR   eggNOG; KOG2314; Eukaryota.
DR   HOGENOM; CLU_011152_4_0_1; -.
DR   InParanoid; E4UZL3; -.
DR   OMA; LWGGPQF; -.
DR   OrthoDB; 5479191at2759; -.
DR   Proteomes; UP000002669; 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; 1.
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   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF036424; eIF3b; 1.
DR   SMART; SM00360; RRM; 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:UP000002669};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03001}.
FT   DOMAIN          38..129
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
SQ   SEQUENCE   745 AA;  84909 MW;  E996361EAD174636 CRC64;
     MSTFDTLTEQ DLQQDEVEID FSDLKAEFEV RLEEGLDTFV VFDGLPIVSE DNKAKLIKFL
     LKKIKKDGPS SSSIDPNRQI FLPMNESGMS EGFAFVEYDT PEEAFAAIKS LHGTPLDKKH
     TLAVNKLTDI DRYGREGRID DEYKPPKIEP FQEKEHLRSW LGDPNARDQF AMYRGDKVGV
     FWNMKKDPPE NIVDRDHWTQ LFVQWSPMGT YLASVHPQGI QLWGGPQFSK QKQFPHPFVQ
     LVEFSPQENY LTTWSSRPIQ IEGAPGVLSY DEDGKNIIVW DITTGKPLRS FVSHDLSAPA
     GTDGDAAPQK KKVQWPAFKW SADEKYVARM LQHQSISVYE LPRMNLLDKT VIKVEGVMDF
     EWSPATVQRE GVKRYEQLLS FWTPEIGSNP AKVGLMSIPS KEIVRTRNLF NVSDVKLHWQ
     SQGAYVCVKV DRHSKSKKSM ATNLEIFRVK EKGVPVEVVD SLKDTVINFA WEPKGDRFVL
     ITTGEAPTGS AVAPKTAVSF FCPEKVKGGA IGNFKLIRTI EKKTSNGIYW SPKGRFVVVA
     TVHSQQNFDL DFWDLDFEGE KPESEKDLSA NLQLMKTIDH FGVTDVDWDP TGRFVISSAS
     AWTHSLENGY NVHTFSGTTL AEHPTEKFKQ LLWRPRPPTL LSKEEQKQVR KNLREYSREF
     DEEDKYAVDI ANTAIVEMRK RVLSEWTAWL RKEKQMILEE REDLGLSPNS DDDIVAQPSI
     TAAEGDTVVE EIVEEIIEET EEIIT
//
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