ID A0A0U1LZ27_TALIS Unreviewed; 1164 AA.
AC A0A0U1LZ27;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=PISL3812_05610 {ECO:0000313|EMBL:CRG88579.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG88579.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG88579.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG88579.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) 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 -!- FUNCTION: Histone methyltransferase that trimethylates histone H3 'Lys-
CC 36' forming H3K36me3. Involved in transcription elongation as well as
CC in transcription repression. {ECO:0000256|ARBA:ARBA00003901}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC Evidence={ECO:0000256|ARBA:ARBA00000317};
CC -!- SUBUNIT: Monomer. Associates with the 60S ribosomal subunit.
CC {ECO:0000256|HAMAP-Rule:MF_03132}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03132}. Nucleus, nucleolus
CC {ECO:0000256|HAMAP-Rule:MF_03132}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Note=Shuttles between cytoplasm and
CC nucleus/nucleolus. {ECO:0000256|HAMAP-Rule:MF_03132}.
CC -!- PTM: Phosphorylation at Ser-1091 and Ser-1092 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; CVMT01000005; CRG88579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1LZ27; -.
DR STRING; 28573.A0A0U1LZ27; -.
DR OMA; EMIDNIM; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000054383; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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 CDD; cd19172; SET_SETD2; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 1.10.1740.100; Set2, Rpb1 interacting domain; 1.
DR HAMAP; MF_00032; eIF_6; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR002769; eIF6.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR025788; Set2_fungi.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044437; SETD2/Set2_SET.
DR InterPro; IPR013257; SRI.
DR InterPro; IPR038190; SRI_sf.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
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; PF17907; AWS; 1.
DR Pfam; PF01912; eIF-6; 1.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF08236; SRI; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00654; eIF6; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR SUPFAM; SSF55909; Pentein; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS51568; SAM_MT43_SET2_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03132};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03132};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CRG88579.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, 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:UP000054383};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_03132};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CRG88579.1}.
FT DOMAIN 145..198
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 200..317
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 324..340
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1091
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03132"
FT MOD_RES 1092
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03132"
SQ SEQUENCE 1164 AA; 129206 MW; 6211076D63FD1804 CRC64;
MPPQDDVKAK PDSAADSGGG GDKIPDSGVP VITEEMEASA LGSPMSVVKD EQPDQSSTPS
VKSGSASVKP EPSDDGPVTS SVGGDITLKQ EPGKPPKLAR SASQKVVARP PQLYDHLPNS
VNEACESFEV IGNCIYSSKY MGHTEHAMEC DCAEEWDGKV NHACGEDSDC INRATRIECL
NDCGCGRDCQ NQRFQRKEYA NVAVIKTAKK GYGLRAESEI RPHQFIYEYI GEVINEGNFR
RRMIQYDKEG IKHFYFMSLN KGEFVDATKK GNLARFCNHS CNPNCYVDKW VVGEKLRMGI
FAERLIQPGE ELVFNYNVDR YGADPQPCYC GEPNCTGFIG GKTQTERATK LSNATIEALG
IEDSEDWDMA VAKRPRKKKT EEPDEEYVES VQPKSLDETG VTKVMAALMQ CAEKWIAVKL
VGRIQRCEDE RALNRVVKMH GYRILNSQLS LWKEDINVVL QILEVLSKLP ALTRNKIIDS
NIESTVRQLT TSEDDRVSKQ STTLLEVWSS LAVGYRIPRM KRDPSATTTQ VVSQFERRET
APGDQRNRSK SRTRSRSRSI EPPRGPAAQT RGGGFAGGGR NAPHNRGPRF PRPPPLPQGW
SERQDVDGRT MYFTANGHSQ YERPTQPAAD MPAAGSLKRK HFREMIDNIM ESRSETPRDK
TSTPGTPQPP KSESRKESWR SYSEEKQKKI YENTIHPHVK YVVDKFKKKL PKDDLKRYAK
EVATKLVDSD FKHGRVEDIT QVSEKQQQKI KKYCKEYFEK AVAKQRAHEK KKADRRQGDS
KSKDTTPHDD TNNINNSNNN KENESDRDFE MDHDGGDSEQ QQEPAAITKR KRDKTDDDDA
EADKGNASPM KRPKSSTPLL DRQSPPSEDE EVEDERLDDE LPHAGLAASS HQSIGTAQFL
DVIILGLAGT ELSTLSTMAV RAQFENSNEV GVFATLTNSY AIVAIGGSEN FYSVFEAELQ
DVIPICHATI GGTRIVGRLT AGNRKGLLVP TSTTDQELQH LRNAIPESVK IQRIEERLSA
LGNVICCNDH VALIHPDLER ETEEIIADVL GVEVFRQTVA DNVLTGSYMA LSNQGGIVHP
KTSIRDQDEL SSLLQVPLVA GSVNRGSPVV GAGMVVNDWL AVTGLDTTAT ELSVVESVFR
LGEMGAKGLG MGNNNKESIV ESFY
//
