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Database: UniProt
Entry: Q7Z0G7
LinkDB: Q7Z0G7
Original site: Q7Z0G7 
ID   SETD7_HALRO             Reviewed;         386 AA.
AC   Q7Z0G7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   05-DEC-2018, entry version 65.
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;
OS   Halocynthia roretzi (Sea squirt) (Cynthia roretzi).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC   Pyuridae; Halocynthia.
OX   NCBI_TaxID=7729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Williamson N.A., Szambelanczyk Orval I., Liu J., Wettenhall R.E.H.;
RT   "Ribosomal protein RL29 is a substrate for rat lysine
RT   methyltransferase SET7/9.";
RL   Submitted (JUN-2002) 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; AY126698; AAM96825.1; -; mRNA.
DR   ProteinModelPortal; Q7Z0G7; -.
DR   SMR; Q7Z0G7; -.
DR   PRIDE; Q7Z0G7; -.
DR   HOVERGEN; HBG028309; -.
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: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; 4.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF037249; Histone_Lys_mtfrase_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; Methyltransferase;
KW   Nucleus; Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    386       Histone-lysine N-methyltransferase SETD7.
FT                                /FTId=PRO_0000316992.
FT   REPEAT       15     38       MORN 1.
FT   REPEAT       39     61       MORN 2.
FT   REPEAT       62     84       MORN 3.
FT   REPEAT      109    131       MORN 4.
FT   DOMAIN      222    344       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      234    236       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00910}.
FT   REGION      302    305       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00910}.
SQ   SEQUENCE   386 AA;  42850 MW;  91997797ABCCF5CB CRC64;
     MDSSDDEIAC DEGDYKGAKD DNDLPHGLGK VKFSSGDEFI GAFEHGIKCG PGKFHFFDDS
     TLEGNYVDGE LHGIGIYTND DGSITKSTYC EGVMEGPSWE YDPEGNITFR GQYSEGVRCG
     LCFYYFPDGG SLIGNVNASG DLSADNIAYI YPDRTTALIG SFEEGDMITA KEANVTITGE
     KGEEISFPTV NSISPDPVYR LDVSTPHVIS TRPLVPDPYE SELVYAAPSK IPNAGEGLYA
     KCDVDQDTVM AFYNGVRLKQ DEVENRDWSQ NSNTISLTDD IAIDVPEEYV STDNYCASLG
     HKVNHSFDPN CRYDIYQHPR FGFIKCVRTI RGVSEGDELT VHYTYEHNDG NKTREAEAPE
     WYKSQLKVFG VDRPAEILEN MDEDYC
//
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