ID F8MMU9_NEUT8 Unreviewed; 957 AA.
AC F8MMU9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 75.
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=NEUTE1DRAFT_122301 {ECO:0000313|EMBL:EGO57973.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO57973.1};
RN [1] {ECO:0000313|EMBL:EGO57973.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO57973.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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; GL891304; EGO57973.1; -; Genomic_DNA.
DR RefSeq; XP_009851047.1; XM_009852745.1.
DR AlphaFoldDB; F8MMU9; -.
DR GeneID; 20824278; -.
DR KEGG; nte:NEUTE1DRAFT122301; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_122301; -.
DR HOGENOM; CLU_008492_0_0_1; -.
DR OrthoDB; 950362at2759; -.
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 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 ECO:0000313|EMBL:EGO57973.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
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:EGO57973.1}.
FT DOMAIN 126..180
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 182..299
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 306..322
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 569..601
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..865
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 107163 MW; 1FA193911BD992F5 CRC64;
MEDGRRSPDS SKESKSEEHS KMNGSKLKRD GASNAGNAAT PNGSQTGNSR HPSMSPDEHK
AASESTATPS ENVPTQKPSR KASQKNMKRE PVLFNHLPDV REEACTHFQV IHDCLYGSKN
MGASEHDALD CDCAEEWRGD MNHACGEDSD CINRATKMEC VDGDCNCGSG CQNQRFQRKQ
YADVSVIKTE KKGFGLRANT DLQVNDFIFE YIGEVINEPT FRSRMVKYDK EGIKHFYFMS
LTKSEFVDAT KKGNLGRFCN HSCDPNCYVD KWVVGDKLRM GIFAGRAIKA GEELVFNYNV
DRYGADPQPC YCGEANCTGF IGGKTQTERA TKLPPATIEA LGIEDGDSWD TAVAATVKKP
RKKKATEDDE EYINRFEPRG LDEEGVTKVM ATLMQCKEKW IAVKLLGRLQ NADDDHVRNR
VVKMHGYQIL KTTLNTFKED TNVVLQILDI LYQLPRITKN KITDSNIEAA VEPLTHSDHE
DVASQSKRLL QEWSKLETAY RIPRKKLDPS APVTTNSFED DRRNVNHEEH PSRPVNPFEN
MVVPTGPRSN IPQRNMNYFN NQRPRKLPTN LPAGWFVTTD STGKYYFYDK SGHTQWQRPT
TPAVDVPKPS AKVEQNQKAL QDIIDSLTKE PTPRHSANQT PKSNTPVPDN GKKEKWRSLP
VEKQMKIYEN TLFPHVKYVM DKFHRRLPKE DLKRFGREIN KKLVASDYKN HRVDDPTTIS
SNQARKIKKF VKDFFDRAVV KHRENEQRAA QKAGPSSSGA PSPTNGGSAM EPKSPLGRNG
ASNAPVKNQQ PDADGDIVLT DVEDEGENTP ATSSPDRKRK RAEEQEVPAP ASEAIPSPKR
AKEDSTTEDS IPSPPPPPPP PTDTPLTEEE RSMREQEEAL MRENEEAQRL EDEEAERRVS
VTVQGAAAAT SKVNGVNGTK AHHTSKASPA VSDESGMDAG RDEKSNKQRV QQEPVSR
//