ID C9SV17_VERA1 Unreviewed; 936 AA.
AC C9SV17;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 91.
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=VDBG_08742 {ECO:0000313|EMBL:EEY22632.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(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; DS985226; EEY22632.1; -; Genomic_DNA.
DR RefSeq; XP_003000946.1; XM_003000900.1.
DR AlphaFoldDB; C9SV17; -.
DR STRING; 526221.C9SV17; -.
DR GeneID; 9534334; -.
DR KEGG; val:VDBG_08742; -.
DR eggNOG; KOG4442; Eukaryota.
DR HOGENOM; CLU_008492_0_1_1; -.
DR OMA; CQEKWIA; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000008698; 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; 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 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 ECO:0000313|EMBL:EEY22632.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698};
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:EEY22632.1}.
FT DOMAIN 113..167
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 169..286
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 293..309
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 562..594
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 104877 MW; 2B3D3BDC57F01AED CRC64;
MEEPKTEDGT VNGLNVKKEE GSSPHGHKLA SRNSSRRRSS SRTPVETKNG TEGVSTPEAT
QGSKSLRKAS QKAAKQEAPT FENYPDMTDD ACATFQRIPD CLYGSKHMGS TDNDALDCDC
REEWQNGENH SCDEDSDCIN RATKMECVMG TGNCGDGCQN QRFQRKAYAD VSVIKTEKKG
FGLRANVDMQ ANDFIFEYIG EVINEPTFRR RMVQYDDEGI KHFYFMSLTK HEFVDATKKG
NLGRFCNHSC NPNCYVDKWV VGDKLRMGIF TLRGIAAGEE LVFNYNVDRY GADPQPCYCG
EPNCTGYIGG KTQTERATKL PLATVEALGI DDGDSWDTAV AKKQRKKKPE EDDEDYVNSV
QARGLDEEGA RKVMASLMQC KEKWIAVKLL ERIQRCDDKQ VLNCVMRMHA YQILRTTLTT
FIDDKNVVAQ VLDILDKFPR LTRNKIQDSK IEATIETLAH SEDPVVAAES KRLLEEWSKL
EVAYRIRRRK VDPKAPAAIN SFEERRNIDR EEDRSKPEPP VVLGADVPKG PRSTIPQRNQ
NFFQGNRPPR RHPAYFQQQQ QGALPEGWFE NTDKRGNVYF YTKNGDTTWQ RPSKPAPDAP
KAISKAKQEQ QLLQSIIQQV TKETPKSSAS RTPQQVDTPV QDPKKEKWRS LPIEKQMKIY
ENTLFPHVKY VLDKYRHKLP KEELKRLGKE VNKTLVSSDY RKNRVEDPTV AINHKKVKTI
KQYVKDFLDR ALIKFKERQS KKSEQTGQTL PASVLPTSDG TGVGESSAPT TSADIPMVDA
DDDVVLSDVD DVETASASSL ERKRKREQLD TGSPDLTPAG SPSAKRVKDD DLDDQAPPPP
PPPPPEAEEM EIGAGAEAVE QQPLTAEQLA LREQEEALMR ENEEAERLEA AERNSSANGA
ARLEEQRLVL NGHVPNGGVI LSGDAAPNDG PPQGGA
//