ID   C1H221_PARBA            Unreviewed;      1028 AA.
AC   C1H221;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 2.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific {ECO:0000256|ARBA:ARBA00018028};
DE            EC=2.1.1.359 {ECO:0000256|ARBA:ARBA00012178};
DE   AltName: Full=SET domain-containing protein 2 {ECO:0000256|ARBA:ARBA00030091};
GN   ORFNames=PAAG_04957 {ECO:0000313|EMBL:EEH33908.2};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH33908.2, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH33908.2, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KN294003; EEH33908.2; -; Genomic_DNA.
DR   RefSeq; XP_015699648.1; XM_015845422.1.
DR   AlphaFoldDB; C1H221; -.
DR   STRING; 502779.C1H221; -.
DR   GeneID; 9096397; -.
DR   KEGG; pbl:PAAG_04957; -.
DR   VEuPathDB; FungiDB:PAAG_04957; -.
DR   eggNOG; KOG4442; Eukaryota.
DR   HOGENOM; CLU_008492_0_1_1; -.
DR   OMA; AQSQPCY; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000002059; Partially assembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd19172; SET_SETD2; 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   InterPro; IPR006560; AWS_dom.
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; IPR017923; TFIIS_N.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR22884:SF413; HISTONE-LYSINE N-METHYLTRANSFERASE CG1716-RELATED; 1.
DR   PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF08711; Med26; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF08236; SRI; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 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.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EEH33908.2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
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:EEH33908.2}.
FT   DOMAIN          148..203
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          205..322
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          329..345
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          602..633
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   REGION          22..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..700
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        785..802
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..830
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..869
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..898
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        900..916
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..947
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        952..966
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..985
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1028 AA;  115262 MW;  991B007C5F673D0E CRC64;
     MALHDDDDIQ PEAVADAVTA LKIKRDNSAE STPIDSTHAS DSANYYPNGF SKSSPTKSIS
     QEQKSQSGSN SPAAKVENGQ PEEKLPVSIT VKLEPGQPPK LSRVGSQKVV PQPAPLFDHL
     PDSTAEATST FQVIDDCTYA NKYMGYTEHA MECDCSEEWD PVAGKNGACG EDSDCINRAT
     KMECVGDCGC GDECQNQRFQ RRQYANVTVI KTEKKGYGLR ADSDLRPHQF IFEYIGEVIN
     EASFRKRMIA YDEEGIKHFY FMSLTKGEFV DATKKGNLGR FCNHSCNPNC YVDKWVVGEK
     LRMGIFAERH IKAGEELVFN YNVDRYGADP QPCYCGEPNC TGFIGGKTQT ERATKLSNAT
     IEALGIDDPD GWDTAVAKRP RKKKTGEDDE EYVDSMQPRS LNEDGVTKVM AALMQCKEKW
     IAVKLLGRIQ RCDDERVRNR VVKMHGYQIL NSQLSAWKDD FNVVLQILDI LDKFPRLTRN
     KIIDSKIEVT IKPLTGCGDE RVEKKAAALL QIWSTLEIGY RIPRMKRDPT ASNNTTAVNR
     FERRESSRND ENQKPRSKSR SRSRSRSIDA PRAPAALRNG KGPPRNSYHH GPRPFRRPPF
     ANPLPQGWFA AESNGKTYYY SASGATTWKR PTAPAPQPPP PPKPESKDKA LQDIIDGIMN
     AKENTPKTRD KSETPATSQP RDAKPPEIKE HKEKWRSYSE EKQKRLYENT IFPHVKYVMD
     KFKHKLPKEE LKRYAKEVGK KLVNSDFKNH RVDDPTKVSD KQIKQIKRYC KEYFDKAVAK
     HLAYEKKKAE RKAREAAKVT EGGSRDATEN PELSQQPEIR DSKKEESDVE EDIKMSDDEM
     DKLEDKKSSP MSLDENSLKR KRDADGNLDV DVDTAGASPS KRTKSSTPPP PPPPPIDMCE
     DVARDSHKRK RDEGGDNGYG TNSFSPGKRT RSESPPPPPP PPPPADTSEM CDAGEDQSRG
     DEEFGIDENT DVNMSSLSSA TPLDHENANR APGKDLNGTL EQQLSLDAFH SLPDETNKVA
     VDVEYCSS
//