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Database: UniProt
Entry: A0A1Y1YPX1_9PLEO
LinkDB: A0A1Y1YPX1_9PLEO
Original site: A0A1Y1YPX1_9PLEO 
ID   A0A1Y1YPX1_9PLEO        Unreviewed;       737 AA.
AC   A0A1Y1YPX1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=BCR34DRAFT_618736 {ECO:0000313|EMBL:ORY00016.1};
OS   Clohesyomyces aquaticus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX   NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORY00016.1, ECO:0000313|Proteomes:UP000193144};
RN   [1] {ECO:0000313|EMBL:ORY00016.1, ECO:0000313|Proteomes:UP000193144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115471 {ECO:0000313|EMBL:ORY00016.1,
RC   ECO:0000313|Proteomes:UP000193144};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-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}.
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:ORY00016.1}.
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DR   EMBL; MCFA01000189; ORY00016.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1YPX1; -.
DR   STRING; 1231657.A0A1Y1YPX1; -.
DR   OrthoDB; 5479191at2759; -.
DR   Proteomes; UP000193144; 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   PIRSF; PIRSF036424; eIF3b; 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:UP000193144};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03001}.
FT   DOMAIN          39..125
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
SQ   SEQUENCE   737 AA;  84830 MW;  D8F97BBA32B853A0 CRC64;
     MAPSYENLPI DDDEFDESQI DFTDIEEQYQ VRLDEGLDAF VVVDGLPVVP EDSKAKLVKF
     LLRKLNSVGK VKDDGVFMPL NDEGKTEGYA FVEYSAPTEA VQAVKQLHAT PLDKRHTMAV
     NKLTDIDRYG KEGRIDEEYY PPEIEPFQQK EHLRSWLGDP EARDQMVFFR GDKVGVMWNE
     KEDPPEPAVD RDNWTESFVQ WSPQGTFLTS MHAQGVQLWG GKAWSRQKRF AHPGVNLVDF
     SPNEKYVTTW SHKPLQVDEN HPVPSLSLED DGKNYVIWDI ATGKPLRSFT TIDVPSTTDA
     EGNPVKKKMQ WPTFKWSSDD KYVARMTQGQ SISVYELPRM NLLDKTSIKI EGVMDFEWAP
     ALPRRDGIKT YEQLFCYWTP ELGSNPAKVG LMSIPSKEIV RTRNLFNVSD AKLHWQSDAA
     YVCVKVDRHS KSKKSMATNL EIFRVREKGV PVEVVDSIKD TVINFAWEPK GNRFVLITTG
     EIPAAGVAVP PKTSVSFFCP EKAKGNVVGN FRHIHTYDKK NSNAIYWSPK GRFVVVAALQ
     SQQSFDLDFY DLSYEKPKDD AEKDKDLTAN LQLMNTAEHY GVTDIEWDPT GRYVATVASA
     FRHHMENGYH MYDFRGNLLR EEHIDRFKQL IWRPRPPTLL SKEEQAEIRK NLRNYSRLFD
     EQDLAKKNTA NRQVVEQRRR LLEEWIAWRK NMIEMLEDEG AEIELNGGVI KMEHDGEVEE
     VEEIVEEIIE ETEEVIS
//
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