ID   A5DAL6_PICGU            Unreviewed;      1055 AA.
AC   A5DAL6;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 2.
DT   02-SEP-2026, entry version 112.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific {ECO:0000256|ARBA:ARBA00015839, ECO:0000256|PIRNR:PIRNR037104};
DE            EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182, ECO:0000256|PIRNR:PIRNR037104};
GN   ORFNames=PGUG_00321 {ECO:0000313|EMBL:EDK36223.2};
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK36223.2, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK36223.2, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Catalytic component of the COMPASS (Set1C) complex that
CC       specifically mono-, di- and trimethylates histone H3 to form
CC       H3K4me1/2/3. COMPASS recognizes ubiquitinated H2B on one face of the
CC       nucleosome which stimulates the methylation of H3 on the opposing face.
CC       {ECO:0000256|PIRNR:PIRNR037104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine =
CC         N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine + 3 H(+); Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537,
CC         Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC         EC=2.1.1.354; Evidence={ECO:0000256|ARBA:ARBA00047571,
CC         ECO:0000256|PIRNR:PIRNR037104};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = N(6)-methyl-L-
CC         lysyl-[histone] + S-adenosyl-L-homocysteine + H(+);
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00905};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC         methionine = N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + S-
CC         adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:60272, Rhea:RHEA-
CC         COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC         ChEBI:CHEBI:61976; Evidence={ECO:0000256|ARBA:ARBA00049129};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC         = N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC         homocysteine + H(+); Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540,
CC         Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC         Evidence={ECO:0000256|ARBA:ARBA00047583};
CC   -!- SUBUNIT: Component of the COMPASS (Set1C) complex.
CC       {ECO:0000256|PIRNR:PIRNR037104}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037104}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000256|PROSITE-ProRule:PRU00905}.
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DR   EMBL; CH408155; EDK36223.2; -; Genomic_DNA.
DR   AlphaFoldDB; A5DAL6; -.
DR   FunCoup; A5DAL6; 136.
DR   STRING; 294746.A5DAL6; -.
DR   KEGG; pgu:PGUG_00321; -.
DR   VEuPathDB; FungiDB:PGUG_00321; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   HOGENOM; CLU_004391_1_0_1; -.
DR   InParanoid; A5DAL6; -.
DR   OMA; ERLPCLC; -.
DR   OrthoDB; 308383at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR   GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR024657; COMPASS_Set1_N-SET.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR044570; Set1-like.
DR   InterPro; IPR017111; Set1_fungi.
DR   InterPro; IPR024636; SET_assoc.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   PANTHER; PTHR45814:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   Pfam; PF11764; N-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF11767; SET_assoc; 1.
DR   PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 1.
DR   SMART; SM01291; N-SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS51572; SAM_MT43_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|PIRNR:PIRNR037104};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|PIRNR:PIRNR037104};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR037104};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR037104};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037104}.
FT   DOMAIN          913..1030
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1039..1055
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          1..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          849..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..716
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..877
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1029
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00190"
SQ   SEQUENCE   1055 AA;  121185 MW;  4C274A3D2E56CFAE CRC64;
     MSYRFKGPDR GDRGDRNDRG GGYHTNYDDK YRREVAPKLS NSYDSFRPSG PRKHNTNHYD
     RDAYYRPMEH RNPSKPAQTP STNPKPEFKP DHEQENGRHS HHGNVQNHTR SPLQPPTPNS
     VTSAPEEVTG TDPRTGVNPH DLKVPTLQLH RDHLQLEFSS PSDPPKNYKV LYDPENDSHR
     NKSTNKSKSK VFRFNGSSVS DPQSYSDAII HSSDITDPRK KILSTYFSKP NKNSKKFPFK
     QLPQPRFVFD KNSVGPPPQT ELVVWDIPST TSEVYVTNFF RSHGNATEIN FLQDPMYAVP
     LGVMSFRFQG SPDKSMLLAK NLLNFVHLEK PKINGVVLKI ELNDHEGKLL RSKVEIAQNR
     IRQSKQKLEM EEQKRREMEE EKKRKEIVAQ REEARQKESQ NNTFQKYDYK PNTTIMSVKY
     RNKVIPGTFL PREVRHIIKD NPYLFIHDKH VSTRTVSAQD IKRVLNKYNW SRVLHEKVGF
     FIIFNSLEEC KRCFWKEDGR RFYEFRMFME MAVPEGFEDK STTSATKGDA VEEATNMLIQ
     EFQAYLKKDI RERVIAPQVL ELLNPERFPV LKAQLDEERT KQAQAAAARA ETIASKIQET
     RNKEGAYALM NKKAAQLPSF KRKEGIKMQA KKRVIPMQHV LNYENDSDDS EDDSSRSATP
     APALKRERSS PATSYDEEAP SKKKKKTSLK TMLLYDSSEG EVSDSPEDQV MEDAEEAADQ
     VDDFADVDVK FRPTLHSSVP VYPEDEFVDE FDVNYIQSSI KDEEDLNIAK SILSELKPST
     IANVDYWAWK QKETRKPEEI AESVHLIEPL APKFESASGS FRSEGYRKIP DTDKIEYLPH
     RRKIYKPVKT VQHEDDETSA NNGNGTNNST AVHSSRVNRA NNRRLVADIS AQKQMLGSET
     DILDLNALTK RKKPVTFARS AIHNWGLYAL ESIAAKEMII EYVGESIRQQ VAEHREKSYL
     KTGIGSSYLF RIDENSVIDA TKKGGIARFI NHCCNPSCTA KIIKVEGKKR IVIYALRDIE
     ANEELTYDYK FERETNDDER IRCLCGAPGC KGYLN
//