ID A0A2J6SWX1_9HELO Unreviewed; 666 AA.
AC A0A2J6SWX1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=K444DRAFT_645992 {ECO:0000313|EMBL:PMD55268.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD55268.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD55268.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD55268.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ613856; PMD55268.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6SWX1; -.
DR STRING; 1095630.A0A2J6SWX1; -.
DR InParanoid; A0A2J6SWX1; -.
DR OrthoDB; 1705992at2759; -.
DR Proteomes; UP000235371; 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 KMT5B-RELATED; 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:UP000235371};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 115..229
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 253..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 75151 MW; B18FE45EBE35DC51 CRC64;
MAPGNTSPKK ERLTLAQLTS YDDILTDALV DHVYYWTNIR KNRNAYHSSR GIKEDEVTSI
LQKRVIIEKD PAKAELELLA LTGLKKFCDA LKTEKEKDDF RKHLRKYINM YLPDCPFEVA
STNRYTVVTQ EASVTARQFI KKGQVVKYLC GIQVIMTEEE EEMIKSSRRD FSIVVSSRNK
SASLFLGPAR FANHDCGANA RLMTSGSAGM EILAVRDIEI GDEITVSYGE NYFGDDNCEC
LCETCEDNCE NGWSAGADGE TKTIPKKSIE EETSSSYSFR NRRRLGSSVS SRNQSETPEV
NIRPHVPKRT PRSLSQFKNQ ESSPLGKSPS REPSESAGTE TPRKRKRELD NLLTPSRQSK
KARPSPLVKM ESNPCFSPPM SSNQSPSSSV QGSRLTSLSP SGTDGQNSTD ATSVDEDTII
VQPRIVSPTV SRLRRSRATK QSPLEQAKSG EPILVGKSTE SSHPVIQDDS DSLLSELNSE
MFDFDDQPTP SKPKEIKKEV EEEDAINTTP KANTTLKKKK SKGTFQPKTD SDHAPPVRKP
GDYVLTHRLL AEPTSAWINC KICEEPFVQQ NAYFTRSSCP RCERHSKLYG YMWPKTDKEG
KDDKEERVLD HRTIHRFVRP SEERTIRKRN RSETESRAVT REISELVVEE VVEKGRKRAK
RSRITM
//
