ID   SETD7_DANRE             Reviewed;         373 AA.
AC   Q6DHG0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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; ORFNames=zgc:92330;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) 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; BC076014; AAH76014.1; -; mRNA.
DR   RefSeq; NP_001002456.1; NM_001002456.1.
DR   AlphaFoldDB; Q6DHG0; -.
DR   SMR; Q6DHG0; -.
DR   STRING; 7955.ENSDARP00000056733; -.
DR   PaxDb; Q6DHG0; -.
DR   GeneID; 436729; -.
DR   KEGG; dre:436729; -.
DR   CTD; 80854; -.
DR   ZFIN; ZDB-GENE-040718-156; setd7.
DR   eggNOG; KOG1079; Eukaryota.
DR   InParanoid; Q6DHG0; -.
DR   OrthoDB; 675418at2759; -.
DR   PhylomeDB; Q6DHG0; -.
DR   BRENDA; 2.1.1.354; 928.
DR   Reactome; R-DRE-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:Q6DHG0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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:0003007; P:heart morphogenesis; IMP:ZFIN.
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   SMART; SM00317; 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..373
FT                   /note="Histone-lysine N-methyltransferase SETD7"
FT                   /id="PRO_0000316990"
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   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   373 AA;  41512 MW;  72F654DB3D7E1033 CRC64;
     MDSDDDNMEE VVEGPLDEDD QPHGFCTVTY SSSDRFEGHF VHGEKNGKGK FFFFDGSTLE
     GFYVDDALQG QGVYTYEDGG ALHGFYVDGE LNGPAQEFNS DGQLVFRGRY KDNIRYGMCW
     VYYPDGACVV GEVNEEGEMT GKAVAYVYPD GRTALYGSFV DGELIEARLA TLTTQENGRP
     HFTVDPDSPI YCYDKSTSSC IAGHKLLPDP YESQRVYVGQ SLISGAGEGL FAQTEAEANT
     VMAFYNGVRI THTEVDSRDW SMNGNTISLD EDTVIDVPAP FNMTENYCGS LGHKANHSFS
     PNCKYDQYVH PRFGQIKCIR TIRAVEKDEE LTVAYGYDHE PSGKSGPEAP EWYTKQFLEF
     QQRESGKGAD ETC