ID A0A1X7VB62_AMPQE Unreviewed; 367 AA.
AC A0A1X7VB62;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Histone-lysine N-methyltransferase SETD7 {ECO:0000256|ARBA:ARBA00020512};
DE EC=2.1.1.364 {ECO:0000256|ARBA:ARBA00023620};
DE AltName: Full=SET domain-containing protein 7 {ECO:0000256|ARBA:ARBA00030095};
GN Name=105311972 {ECO:0000313|EnsemblMetazoa:Aqu2.1.37540_001};
OS Amphimedon queenslandica (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Haplosclerida; Niphatidae; Amphimedon.
OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.37540_001, ECO:0000313|Proteomes:UP000007879};
RN [1] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20686567; DOI=10.1038/nature09201;
RA Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The Amphimedon queenslandica genome and the evolution of animal
RT complexity.";
RL Nature 466:720-726(2010).
RN [2] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT evolution of animal complexity.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.37540_001}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2017) to UniProtKB.
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:0000256|ARBA:ARBA00023564};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000256|ARBA:ARBA00034257};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737;
CC Evidence={ECO:0000256|ARBA:ARBA00034257};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_011402540.1; XM_011404238.2.
DR AlphaFoldDB; A0A1X7VB62; -.
DR STRING; 400682.A0A1X7VB62; -.
DR EnsemblMetazoa; Aqu2.1.37540_001; Aqu2.1.37540_001; Aqu2.1.37540.
DR GeneID; 105311972; -.
DR KEGG; aqu:105311972; -.
DR eggNOG; KOG1079; Eukaryota.
DR InParanoid; A0A1X7VB62; -.
DR OMA; RITHTEV; -.
DR OrthoDB; 5304435at2759; -.
DR Proteomes; UP000007879; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140945; F:histone H3K4 monomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd10530; SET_SETD7; 1.
DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR017155; Hist-Lys_N-MeTrfase_SETD7.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044436; SETD7_SET.
DR PANTHER; PTHR46820; HISTONE-LYSINE N-METHYLTRANSFERASE SETD7; 1.
DR PANTHER; PTHR46820:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SETD7; 1.
DR Pfam; PF02493; MORN; 2.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51577; SAM_MT43_SET7; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007879};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 223..346
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..29
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"
SQ SEQUENCE 367 AA; 41244 MW; 05EDAF494931E602 CRC64;
MEEENEEIEE EEEPLYVGQR DAEGNPNGRG TLKWLKSSRR FEGRFCSGMK QGRGCFYFKD
GSSLSGTFRS DELHGEGTYT YPDGRLMIAQ YVNGELDGPF TEYSETGDVM AKGEHREDRR
FGFLQIFDEY GGILMGEVNR DTGELTGPGI AYVYPDKRSA LLGRFSNSDM VCARPALLLT
SVDQTPAKYA LDENWSKTTL KLDESTSTCI SCNPLTPDAY EQSKVYVSTC SDNPDKGEGL
FAKTELAEGE TVSFYNGLRL THDEVDSRDW SLNANTITLD ESMVLDVPLK YSSLDAYVAS
LGHKANHSSA PNCEYDHFVH PRFGHIKCIR TIKEVSKGNE LTCDYGYSHK LPETDEEDLP
EWYMTES
//
