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Database: UniProt
Entry: A0A061AWA0_CYBFA
LinkDB: A0A061AWA0_CYBFA
Original site: A0A061AWA0_CYBFA 
ID   A0A061AWA0_CYBFA        Unreviewed;       721 AA.
AC   A0A061AWA0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=BON22_3410 {ECO:0000313|EMBL:ONH66774.1}, CYFA0S_02e09340g
GN   {ECO:0000313|EMBL:CDR38952.1};
OS   Cyberlindnera fabianii (Yeast) (Hansenula fabianii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=36022 {ECO:0000313|EMBL:CDR38952.1};
RN   [1] {ECO:0000313|EMBL:CDR38952.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YJS4271 {ECO:0000313|EMBL:CDR38952.1};
RX   PubMed=25103752; DOI=10.1128/genomeA.00638-14;
RA   Freel K.C., Sarilar V., Neuveglise C., Devillers H., Friedrich A.,
RA   Schacherer J.;
RT   "Genome sequence of the yeast Cyberlindnera fabianii (Hansenula
RT   fabianii).";
RL   Genome Announc. 2:E00638-E00638(2014).
RN   [2] {ECO:0000313|Proteomes:UP000189513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65 {ECO:0000313|Proteomes:UP000189513};
RX   PubMed=28385833; DOI=10.1128/genomeA.00064-17;
RA   van Rijswijck I.M.H., Derks M.F.L., Abee T., de Ridder D., Smid E.J.;
RT   "Genome sequences of Cyberlindnera fabianii 65, Pichia kudriavzevii 129,
RT   and Saccharomyces cerevisiae 131 isolated from fermented masau fruits in
RT   Zimbabwe.";
RL   Genome Announc. 5:E00064-E00064(2017).
RN   [3] {ECO:0000313|EMBL:ONH66774.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65 {ECO:0000313|EMBL:ONH66774.1};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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; LK052887; CDR38952.1; -; Genomic_DNA.
DR   EMBL; MPUK01000006; ONH66774.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061AWA0; -.
DR   STRING; 36022.A0A061AWA0; -.
DR   VEuPathDB; FungiDB:BON22_3410; -.
DR   OMA; LWGGPQF; -.
DR   OrthoDB; 5479191at2759; -.
DR   Proteomes; UP000189513; 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:UP000189513};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03001}.
FT   DOMAIN          33..116
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
SQ   SEQUENCE   721 AA;  82757 MW;  4CF43EE57C9E0CA5 CRC64;
     MEPPKIEDIR LDDVDFTDLE EQFAVPEDTT FERYVVVDGA PVAPEAKAAV LTKVLTKLFN
     GAGKVTNLHM PIEAGKTKGF CFVEFETPQQ VEKAIKQLNG KKLDVKHRLF LNRLSDIEKY
     AIDGAVSDEF VPPPFPEFKE TDYLKSWLQD EAGRDQFLMH KGDVTGIFWS KKDQAEPAIE
     PREHWTQGPI KFSPQGQYLF TMHPQGVQAW GGASFSNLKK FSHPGVRLLD FSPSERYLVT
     LSPEPLQTPP DDHPRRATYP FGPESDGHKL VIWDIVSGLP VRTFPLPPHL EQKREMIWPL
     VKWSYDDKYV ARMGPGALAI YDTTDNFALV DKKPIKIDDL QDFEFAPAGV KFANHRQQDP
     LAHVLAYWTP ETANQTAKVS ILEVPSKKVI RTTNLVQVTD IKLHWQDQGE YLLAKVDRHT
     KSKKTIFTNM EIFKLNEKDV PVEKVELKDR VVNFQWEPNG DRFVTISRPE EADPNPSIPK
     NVISFWAPEL SKAKVAPLKK WIAFKKFENK FNNTLNFSPR GRFIAISVIG QSASKGSIEF
     FDLDYTGEKK EGEPTNVDAH VKLLATEAYG GVTDVEWDPS GRFLAAWSSV WRHKIENGYK
     IFDFGGRLLR DELVDDFKVF MWRPRPESLL KGGDKKKVRK NLREYSAQFD EIDAMEQSTA
     ARELILTRRR LLEEWTSWRS TIESHKEDYG IVEQTSNEED EEVIEEIMEE IVDEKEEIVE
     E
//
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