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Database: UniProt
Entry: C1G686_PARBD
LinkDB: C1G686_PARBD
Original site: C1G686_PARBD 
ID   C1G686_PARBD            Unreviewed;       248 AA.
AC   C1G686;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 2.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Eukaryotic translation initiation factor 6 {ECO:0000256|HAMAP-Rule:MF_03132};
DE            Short=eIF-6 {ECO:0000256|HAMAP-Rule:MF_03132};
GN   Name=TIF6 {ECO:0000256|HAMAP-Rule:MF_03132};
GN   ORFNames=PADG_02691 {ECO:0000313|EMBL:EEH46593.2};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH46593.2, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH46593.2, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH46593.2,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
CC   -!- FUNCTION: Binds to the 60S ribosomal subunit and prevents its
CC       association with the 40S ribosomal subunit to form the 80S initiation
CC       complex in the cytoplasm. Is also involved in ribosome biogenesis.
CC       Associates with pre-60S subunits in the nucleus and is involved in its
CC       nuclear export. {ECO:0000256|HAMAP-Rule:MF_03132}.
CC   -!- SUBUNIT: Monomer. Associates with the 60S ribosomal subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_03132}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03132}.
CC       Nucleus, nucleolus {ECO:0000256|HAMAP-Rule:MF_03132}. Note=Shuttles
CC       between cytoplasm and nucleus/nucleolus. {ECO:0000256|HAMAP-
CC       Rule:MF_03132}.
CC   -!- PTM: Phosphorylation at Ser-168 and Ser-169 promotes nuclear export.
CC       {ECO:0000256|HAMAP-Rule:MF_03132}.
CC   -!- SIMILARITY: Belongs to the eIF-6 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03132}.
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DR   EMBL; KN275959; EEH46593.2; -; Genomic_DNA.
DR   RefSeq; XP_010758087.1; XM_010759785.1.
DR   AlphaFoldDB; C1G686; -.
DR   STRING; 502780.C1G686; -.
DR   GeneID; 22582128; -.
DR   KEGG; pbn:PADG_02691; -.
DR   VEuPathDB; FungiDB:PADG_02691; -.
DR   eggNOG; KOG3185; Eukaryota.
DR   HOGENOM; CLU_071894_0_0_1; -.
DR   InParanoid; C1G686; -.
DR   OMA; LCHPKAT; -.
DR   OrthoDB; 5473211at2759; -.
DR   Proteomes; UP000001628; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042256; P:cytosolic ribosome assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IEA:UniProtKB-UniRule.
DR   CDD; cd00527; IF6; 1.
DR   HAMAP; MF_00032; eIF_6; 1.
DR   InterPro; IPR002769; eIF6.
DR   NCBIfam; TIGR00323; eIF-6; 1.
DR   PANTHER; PTHR10784; EUKARYOTIC TRANSLATION INITIATION FACTOR 6; 1.
DR   PANTHER; PTHR10784:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 6; 1.
DR   Pfam; PF01912; eIF-6; 1.
DR   PIRSF; PIRSF006413; IF-6; 1.
DR   SMART; SM00654; eIF6; 1.
DR   SUPFAM; SSF55909; Pentein; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03132};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_03132}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03132};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03132};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_03132}; Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_03132}.
FT   MOD_RES         168
FT                   /note="Phosphoserine; by CK1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03132"
FT   MOD_RES         169
FT                   /note="Phosphoserine; by CK1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03132"
SQ   SEQUENCE   248 AA;  26435 MW;  58D6CE39E348BF18 CRC64;
     MAVRARVGVF ATLTNSYALV AIGSSENFYS VFEAELQDVI PICHATIAGT RIVGRLTAGN
     RKGLLVPTST TDQELQHLRN SLPDAVKIQR IEERLTALGN VICCNDHVAL VHPDIERETE
     EIISDVLGVE VFRQTIADNV LTGSYMSLSN QGGIVHPKTS IQDQDELSSL VQVPLVAGSV
     NRGSPVIGAG MVVNDWLAVT GMDTTATELS VVESVFKLGE GAPGAVAGKN FIGAFGNTHK
     ESLVESFY
//
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