GenomeNet

Database: UniProt
Entry: Q6DHG0
LinkDB: Q6DHG0
Original site: Q6DHG0 
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   16-JAN-2019, entry version 89.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD7;
DE            EC=2.1.1.43;
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   Cyprinidae; 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
CC       monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation
CC       represents a specific tag for epigenetic transcriptional
CC       activation. Plays a central role in the transcriptional activation
CC       of genes. Has also methyltransferase activity toward non-histone
CC       proteins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00910};
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00910}.
DR   EMBL; BC076014; AAH76014.1; -; mRNA.
DR   RefSeq; NP_001002456.1; NM_001002456.1.
DR   UniGene; Dr.83856; -.
DR   ProteinModelPortal; 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   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000074731; -.
DR   HOVERGEN; HBG028309; -.
DR   InParanoid; Q6DHG0; -.
DR   KO; K11431; -.
DR   OrthoDB; 675418at2759; -.
DR   PhylomeDB; Q6DHG0; -.
DR   PRO; PR:Q6DHG0; -.
DR   Proteomes; UP000000437; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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   InterPro; IPR017155; Hist-Lys_N-MeTrfase_SET.
DR   InterPro; IPR003409; MORN.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF02493; MORN; 3.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF037249; Histone_Lys_mtfrase_SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51577; SAM_MT43_SET7; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Activator; Chromatin regulator; Chromosome; Complete proteome;
KW   Methyltransferase; Nucleus; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN         1    373       Histone-lysine N-methyltransferase SETD7.
FT                                /FTId=PRO_0000316990.
FT   REPEAT       36     58       MORN 1.
FT   REPEAT       59     81       MORN 2.
FT   REPEAT      106    128       MORN 3.
FT   DOMAIN      214    336       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      226    228       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00910}.
FT   REGION      294    297       S-adenosyl-L-methionine binding.
FT                                {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
//
DBGET integrated database retrieval system