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Database: UniProt/TrEMBL
Entry: F8MMU9_NEUT8
LinkDB: F8MMU9_NEUT8
Original site: F8MMU9_NEUT8 
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
//
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