SETD7_XENTR
ID SETD7_XENTR Reviewed; 366 AA.
AC Q4QQN5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Histone-lysine N-methyltransferase SETD7;
DE EC=2.1.1.364 {ECO:0000250|UniProtKB:Q8WTS6, ECO:0000255|PROSITE-ProRule:PRU00910};
DE AltName: Full=SET domain-containing protein 7;
GN Name=setd7;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone methyltransferase that specifically monomethylates
CC 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag
CC for epigenetic transcriptional activation. Plays a central role in the
CC transcriptional activation of genes. Has also methyltransferase
CC activity toward non-histone proteins.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000250|UniProtKB:Q8WTS6, ECO:0000255|PROSITE-
CC ProRule:PRU00910};
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET7 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00910}.
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DR EMBL; BC098189; AAH98189.1; -; mRNA.
DR RefSeq; NP_001027510.1; NM_001032339.1.
DR AlphaFoldDB; Q4QQN5; -.
DR SMR; Q4QQN5; -.
DR STRING; 8364.ENSXETP00000036910; -.
DR PaxDb; Q4QQN5; -.
DR GeneID; 613102; -.
DR KEGG; xtr:613102; -.
DR CTD; 80854; -.
DR Xenbase; XB-GENE-949196; setd7.
DR eggNOG; KOG1079; Eukaryota.
DR HOGENOM; CLU_803117_0_0_1; -.
DR InParanoid; Q4QQN5; -.
DR OMA; NGIRITH; -.
DR OrthoDB; 675418at2759; -.
DR PhylomeDB; Q4QQN5; -.
DR TreeFam; TF106392; -.
DR Reactome; R-XTR-3214841; PKMTs methylate histone lysines.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR ExpressionAtlas; Q4QQN5; differential.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0070828; P:heterochromatin organization; IBA:GO_Central.
DR GO; GO:0034968; P:histone lysine methylation; IEA:InterPro.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd10530; SET_SETD7; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR017155; Hist-Lys_N-MeTrfase_SET.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044436; SETD7_SET.
DR Pfam; PF02493; MORN; 3.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF037249; Histone_Lys_mtfrase_SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51577; SAM_MT43_SET7; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Activator; Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..366
FT /note="Histone-lysine N-methyltransferase SETD7"
FT /id="PRO_0000316991"
FT REPEAT 36..58
FT /note="MORN 1"
FT REPEAT 59..81
FT /note="MORN 2"
FT REPEAT 106..128
FT /note="MORN 3"
FT DOMAIN 214..336
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 226..228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00910"
FT BINDING 294..297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00910"
SQ SEQUENCE 366 AA; 40816 MW; 9470B465CFFD2F4B CRC64;
MDSEDETVEE TVEGLLDDDG LPHGFCTVNY SSTDRFEGHF VHGEKNGRGK FYFFDGSTLE
GFYVDDALQG QGIYTYEDGG SLHGTYVEGE LNGPAQEYDT DGRLIFKGQY KDNVRHGVCW
IYYPDGGSLV GEVNEDGDMT GDKVAYVYPD GRMALYGKFI DAEMLEGKLA ILTSVDEGKP
HFELVPNGPV YNFDKSTPSC ISVNPLFPDP YESERVYVND SLIHNAGEGL FAKVASAAQT
VMSFYNGVRI THQEVDSREW ALNGNTISLD DETVLDVPAP YNSYYKYCAS LGHKANHSFS
PNCMYDTFVH PRFGPIKCIR TMKAVEKDEE LTVAYGYDHS VTGKNGPEAP EWYQQQLTAF
QATQQK