ID G9KNA1_MUSPF Unreviewed; 353 AA.
AC G9KNA1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
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};
DE Flags: Fragment;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|EMBL:AES06380.1};
RN [1] {ECO:0000313|EMBL:AES06380.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lungs {ECO:0000313|EMBL:AES06380.1};
RX PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA Farooqui A., Kelvin D.J.;
RT "Sequencing, annotation, and characterization of the influenza ferret
RT infectome.";
RL J. Virol. 87:1957-1966(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JP017782; AES06380.1; -; mRNA.
DR AlphaFoldDB; G9KNA1; -.
DR HOGENOM; CLU_803117_0_0_1; -.
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; 3.
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; 4.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF037249; Histone_Lys_mtfrase_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 2: Evidence at transcript level;
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR037249-1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 202..324
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT BINDING 214..216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-1"
FT BINDING 284
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-1"
FT BINDING 285
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-1"
FT BINDING 344
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-1"
FT SITE 233
FT /note="Histone H3K4 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-2"
FT SITE 244
FT /note="Histone H3K4 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-2"
FT SITE 254
FT /note="Histone H3K4 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-2"
FT SITE 305
FT /note="Histone H3K4 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-2"
FT SITE 323
FT /note="Histone H3K4 binding"
FT /evidence="ECO:0000256|PIRSR:PIRSR037249-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AES06380.1"
FT NON_TER 353
FT /evidence="ECO:0000313|EMBL:AES06380.1"
SQ SEQUENCE 353 AA; 39235 MW; EB536B394C59D911 CRC64;
EGHLDDDGLP HGFCTVTYSS TDRFEGNFVH GEKNGRGKFF FFDGSTLEGY YVDDALQGQG
VYTYEDGGVL QGTYVDGELN GPAQEYDTDG RLIFKGQYKD NIRHGVCWIY YPDGGSLVGE
VNEDGEMTGE KIAYVYPDER TALYGKFIDG EMIEGKLATL MSTEEGRPHF ELVPGSSVYH
FDKSTSSCIS TRALLPDPYE SERVYVAESL ISSAGEGLFS KVAVGPNTVM SFYNGVRITH
QEVDSRDWAL NGNTLSLDEE TVIDVPEPYN HVSKYCASLG HKANHSFTPN CIYDMFVHPR
FGPIKCIRTL RAVEAEEELT VAYGYDHSPP GKNGPEAPEW YQVELKAFQA AQQ
//
