ID A6RCK0_AJECN Unreviewed; 246 AA.
AC A6RCK0;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=HCAG_07358 {ECO:0000313|EMBL:EDN10897.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN10897.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476662; EDN10897.1; -; Genomic_DNA.
DR AlphaFoldDB; A6RCK0; -.
DR STRING; 339724.A6RCK0; -.
DR VEuPathDB; FungiDB:HCAG_07358; -.
DR HOGENOM; CLU_040002_1_1_1; -.
DR OrthoDB; 1705992at2759; -.
DR Proteomes; UP000009297; 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 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 KMT5B-RELATED; 1.
DR PANTHER; PTHR12977; SUPPRESSOR OF VARIEGATION 4-20-RELATED; 1.
DR Pfam; PF00856; 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:UP000009297};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 116..231
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
SQ SEQUENCE 246 AA; 28176 MW; D060E9DCE79EE057 CRC64;
MAPKIPPPDR KEKLTLSQLA SYDDVITDAL VDRAYFWTKI RKNRTKYISC RGILEEQVTA
ILLHDVIVGK DVPKAEKALL AIPGLKKFVD RLKSDREKEW FRRHLRKYIS IYLPDCPFEV
MTTKSLYHNH PRSGCFLRAS TSPRGTTIRG LSGTLVPMTR EEEIDLDLTR KDFSIVMSSR
KKTPSIFLGP ARFANHDCNA NARLVMRGPE SMEVVAIRDI VVGEEITVSY GENYFEGGKW
SERLRT
//
