ID A0A178EK16_9PLEO Unreviewed; 246 AA.
AC A0A178EK16;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 17.
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=IQ07DRAFT_557059 {ECO:0000313|EMBL:OAL55539.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL55539.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL55539.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL55539.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV441637; OAL55539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EK16; -.
DR STRING; 765867.A0A178EK16; -.
DR InParanoid; A0A178EK16; -.
DR OrthoDB; 5473211at2759; -.
DR Proteomes; UP000077535; 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:UP000077535};
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 246 AA; 26369 MW; 07D89199EE55E65D CRC64;
MAVRAQFENS NEVGVFSTLT NAYAIVAVGA SENFYSVFEA ELQDVIPICH ATIAGTRIVG
RLTAGNKKGL LVPTTTTDQE LQHLRNSIPD SVKIQRIEER LSALGNVICC NDHVALVHPD
IERETEEIIA DVLGVEVFRQ TIADNVLTGS YMALSNQGGI VHPKTSIQDQ DELSSLLQVP
LVAGSVNRGS AVVGAGMVVN DWMAVTGLDT TATELSVVES VFRLGEGNGP SNINTTHKDA
MVESFY
//