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Database: UniProt
Entry: A0A420Y1F5_9PEZI
LinkDB: A0A420Y1F5_9PEZI
Original site: A0A420Y1F5_9PEZI 
ID   A0A420Y1F5_9PEZI        Unreviewed;       938 AA.
AC   A0A420Y1F5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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   Name=SET2 {ECO:0000313|EMBL:RKU41757.1};
GN   ORFNames=DL546_002181 {ECO:0000313|EMBL:RKU41757.1};
OS   Coniochaeta pulveracea.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=177199 {ECO:0000313|EMBL:RKU41757.1, ECO:0000313|Proteomes:UP000275385};
RN   [1] {ECO:0000313|EMBL:RKU41757.1, ECO:0000313|Proteomes:UP000275385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAB683 {ECO:0000313|EMBL:RKU41757.1,
RC   ECO:0000313|Proteomes:UP000275385};
RA   Borstlap C.J., De Witt R.N., Botha A., Volschenk H.;
RT   "Draft genome of the lignicolous fungus Coniochaeta pulveracea.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RKU41757.1}.
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DR   EMBL; QVQW01000068; RKU41757.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420Y1F5; -.
DR   STRING; 177199.A0A420Y1F5; -.
DR   Proteomes; UP000275385; 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; 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; 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; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:RKU41757.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275385};
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:RKU41757.1}.
FT   DOMAIN          126..179
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          181..298
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          305..321
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          564..596
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          737..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..648
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..803
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..839
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..928
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   938 AA;  105884 MW;  E7BBC436038A996C CRC64;
     MGTVKKEEDE RSAEVMMDDV RLDEPAPING SRVKNERHSA STTPNGLDTK SPRANALFDD
     PAVKNETESS IPENRPPKLS RKQSHKATST PMLFDQLPDA TRDACEAFQV INDCLYGSRN
     LGTSNSEPMD CDCAEEWYDG QNHACSEDGA CINRVVKMEC MNDCNCGAGC QNQRFQKKEY
     ADVSVIKTEK KGFGLRANAV LEANDFIFEY IGEVINEPTF RRRMLQYDQE GIKHFYFMSL
     NKGEFVDATK KGNLGRFCNH SCNPNCYVDK WIVGDKVRMG IFAGRKISVG EELVFNYNVD
     RYGADPQPCY CGEPNCTGYI GGKTQTERAT KLPVATIEAL GIEDGDSWDT AVAKKPRKKK
     VTEDDEDYVN SVQARGLDEA GVTKVMPALM QCKEKWIAVK LLERIQNAED DRVRHQVVRM
     HGYQILKTTL ETFKDDTNVV LQILDVLYQL PRLTKNKITE AKIEGPIQSL TSSENEEVAA
     GAKRLLDVWS KLETAYRIPR QKADSHAPAV NAFDERRNMR REAETAKPDP FANVVIPKGP
     RSNVPQRSAP FFGGAPRPRK VPPSNIPAGW YIATDPSGAY YFYNKKGETT WRKPTEPAVE
     VATVPSKVQD KEKALQDIIN NLTKDPTPRQ SATHTPQRGN TPAQETKQEK WRSLPIEKQM
     RIYENTISPH VSHVMNKFRH KLPKDELKRL AKEISKKLVA SDYKNKRVKD PTTMSEDKAR
     GVKNYVKGFF DRAVVKHREH EKRKAERDAQ TIAQAPPDAL AEPAASEGLP AQVDDEVILT
     DVEDEDASVD SAERKRKRDG EEAGSANQTP SDTPSLKRVK EEDAVTPPPP PPPPPATDTP
     TMEMTEEERF MKEQEEALMR ENEEAERLEE AEQSKLREQV SVLEQRNEEA RRDNAVHEEL
     TGEEKPRTNG NHERMEIDES KDSMDSQQEG RTRQVLSH
//
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