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Database: UniProt/TrEMBL
Entry: G3BBE8_CANTC
LinkDB: G3BBE8_CANTC
Original site: G3BBE8_CANTC 
ID   G3BBE8_CANTC            Unreviewed;       721 AA.
AC   G3BBE8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 73.
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=CANTEDRAFT_99232 {ECO:0000313|EMBL:EGV62172.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV62172.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(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; GL996527; EGV62172.1; -; Genomic_DNA.
DR   RefSeq; XP_006688342.1; XM_006688279.1.
DR   AlphaFoldDB; G3BBE8; -.
DR   STRING; 590646.G3BBE8; -.
DR   GeneID; 18250839; -.
DR   KEGG; cten:CANTEDRAFT_99232; -.
DR   eggNOG; KOG4442; Eukaryota.
DR   HOGENOM; CLU_008492_1_1_1; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000000707; Unassembled 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   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 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; IPR035441; TFIIS/LEDGF_dom_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   Pfam; PF00397; WW; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000707};
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}.
FT   DOMAIN          51..107
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          109..226
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          233..249
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          476..510
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   REGION          436..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..721
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   721 AA;  82668 MW;  7FBE5BD8D3318D23 CRC64;
     MSESEDDKQQ QRRTPPVFLD CESATEEALQ TFTQITACSY QNKSIGDSGQ NENMTCDCHE
     KVEETTNVNH ACGDDSGCIN RATSVECMAG ACNCGDRCQN QRFQRCEYAA ISVFQTEKKG
     YGVRADTALD EGSFIYEYIG EVIDEATFRR RMVDYDSRQL RHFYFMMLKK DAFIDATEKG
     ALARFVNHSC SPNAYVDKWV VGDKLRMGIF AKRHIARGEE ITFDYNVDRY GAQSQPCYCG
     EPNCIKFMGG KTQTDAALLL PDGISEALGV TPRHERQWLK ENKHLRTKQQ NNDATINEAF
     VKSVEVSEIE EQDVNRVMAA MMKSHDANIN RKLVERIYLT DDENVNRQIV RMHGYKTLSA
     LLKSQTTDPD TTVKILKVLA KWPKMTRNKI QSSQIEDVVK DIRAHTNNRE IRSLSVALLD
     EWGKLQMAYR IPKVSHSDAG QISYGRNPRS SSPEKLQDPN PVKHEEPEPQ DPSSQTELPP
     GWESALDPNT NTMYYFNRDL GETTWERPQV KPKLKLKPVP VPRGPRQDSP PQRSTNNYNE
     SQIAEMEAQR LDQEKQMLWQ QNLNKQKSLQ ELILQSQREA EERKAMDLRL KQELTDKARA
     RAKAKSKVKG SKSSGTTSSV EKRWSSLFAK YVPNLIKKHT EEIGKDNVKQ CAREMVKVLV
     MKEMNKDATR EPPADFEKSK LKQVKEFTGS YMDKFMIKYR QKHSKRHGEE TEGTIKRTKL
     T
//
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