ID B6Q950_TALMQ Unreviewed; 640 AA.
AC B6Q950;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 08-NOV-2023, entry version 65.
DE RecName: Full=Histone-lysine N-methyltransferase SET9 {ECO:0000256|ARBA:ARBA00015413};
DE EC=2.1.1.372 {ECO:0000256|ARBA:ARBA00024057};
DE AltName: Full=Histone-lysine N-methyltransferase set9 {ECO:0000256|ARBA:ARBA00014232};
DE AltName: Full=SET domain protein 9 {ECO:0000256|ARBA:ARBA00030653};
GN ORFNames=PMAA_070880 {ECO:0000313|EMBL:EEA26004.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA26004.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- FUNCTION: Histone methyltransferase that trimethylates 'Lys-20' of
CC histone H4 to form H4K20me3. {ECO:0000256|ARBA:ARBA00001984}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:64456, Rhea:RHEA-COMP:15554, Rhea:RHEA-
CC COMP:15998, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.372;
CC Evidence={ECO:0000256|ARBA:ARBA00023940};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS995900; EEA26004.1; -; Genomic_DNA.
DR RefSeq; XP_002146551.1; XM_002146515.1.
DR AlphaFoldDB; B6Q950; -.
DR STRING; 441960.B6Q950; -.
DR VEuPathDB; FungiDB:PMAA_070880; -.
DR HOGENOM; CLU_013724_0_0_1; -.
DR OrthoDB; 1705992at2759; -.
DR PhylomeDB; B6Q950; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140943; F:histone H4K20 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd10524; SET_Suv4-20-like; 1.
DR Gene3D; 1.10.10.1700; Histone-lysine N-methyltransferase; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR041938; Hist-Lys_N-MTase_N.
DR InterPro; IPR025783; Set9_fungi.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR039977; Suv4-20/Set9.
DR PANTHER; PTHR12977:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE SUV4-20; 1.
DR PANTHER; PTHR12977; SUPPRESSOR OF VARIEGATION 4-20-RELATED; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51567; SAM_MT43_SUVAR420_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW Transferase {ECO:0000256|ARBA:ARBA00022603}.
FT DOMAIN 119..233
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 272..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 72235 MW; 4399EF3821F765BC CRC64;
MSSKARSTPV ADSRDRLTLS RLANYDDVAT DALIDRAYFW TTIRKNRTKF APGRGILEDV
VTKILLHKVI VEKNPRAAEQ ELLAMKGLKK YLDSLPNDRE REWFKRHFRK YIHIYLPDCP
FEISTTNRYT IIEHEASVVA RRNIKKGEEI KYLCGTLVSM TRQEELDLGF NRKDFSIVMS
SRRKNPSLFL GPARFANHDC NANGRLSTRG NDGMQVIAAR DIELGEEITV SYGEDYFGID
NCECLCETCE RTVRNGWSPA VSVPTSLVST PFRDAEIDPS NPKKENHASQ TVQLPGNDAH
VATETITMSE TEHNGKRKFN SDSDSELSSP STPNKRFKFE HRQSKLREEL LLSEVAESIE
KSPIPVTAQG PPQPIPTLQS PPDQTISTDA EQNTASSTEN DSPSYSSDES NPSISTPATS
VSGIAPDIKI ESIETSTVPA VSGSSSIQQS PGKDITNITD TSIAQSSQIS EVNERKSRSR
TSTPRKRALP SVEQVDIIVN RVPGDYTRTD MLLAQRYDRW VDCRTCSAWF VQENAYQTRK
ECPRCERHSK LYGYRWPKTD PEGSPDEDPR VMDHRTVHRF LSAEEEAKVD RKHRSGVVTP
TPTPEIIPLD TRSETEFSDY EGRRLTRASR IRARSLRLTQ
//