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   03-AUG-2022, entry version 74.
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   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 methyltransferase
RT   SET7/9.";
RL   Submitted (JUN-2002) 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; AY126698; AAM96825.1; -; mRNA.
DR   AlphaFoldDB; Q7Z0G7; -.
DR   SMR; Q7Z0G7; -.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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; 4.
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   Repeat; S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN           1..386
FT                   /note="Histone-lysine N-methyltransferase SETD7"
FT                   /id="PRO_0000316992"
FT   REPEAT          15..38
FT                   /note="MORN 1"
FT   REPEAT          39..61
FT                   /note="MORN 2"
FT   REPEAT          62..84
FT                   /note="MORN 3"
FT   REPEAT          109..131
FT                   /note="MORN 4"
FT   DOMAIN          222..344
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         234..236
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00910"
FT   BINDING         302..305
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="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