ID A5DJM0_PICGU Unreviewed; 245 AA.
AC A5DJM0;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=PGUG_03471 {ECO:0000313|EMBL:EDK39373.1};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK39373.1, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK39373.1, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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-174 and Ser-175 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; CH408158; EDK39373.1; -; Genomic_DNA.
DR RefSeq; XP_001484090.1; XM_001484040.1.
DR AlphaFoldDB; A5DJM0; -.
DR STRING; 294746.A5DJM0; -.
DR GeneID; 5126407; -.
DR KEGG; pgu:PGUG_03471; -.
DR VEuPathDB; FungiDB:PGUG_03471; -.
DR eggNOG; KOG3185; Eukaryota.
DR HOGENOM; CLU_071894_0_0_1; -.
DR InParanoid; A5DJM0; -.
DR OMA; LCHPKAT; -.
DR OrthoDB; 5473211at2759; -.
DR Proteomes; UP000001997; 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:UP000001997};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_03132}.
FT MOD_RES 174
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03132"
FT MOD_RES 175
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03132"
SQ SEQUENCE 245 AA; 26360 MW; 77D87F39B6B4CAEB CRC64;
MATRTQFENS NEVGVFAKLT NSYALVAVGG SENFYSAFEA ELGDVIPIVH TTIAGTRIVG
RMTAGNRRGL LVPTQTTDQE LMHLRNSLPD SVKIQRVEER LSALGNVICC NDYVALVHPD
IERETEELIA DVLGVEVFRQ TIAGNVLVGS YCALSNQGGI VHPQTSIQDQ EELSSLLQVP
LVAGTVNRGS SVVGAGMVVN DWLSVAGLDT TAPELSVIES IFRLQDAQPD SISGNLRDTL
IETYS
//
