ID A0A091G2D9_9AVES Unreviewed; 267 AA.
AC A0A091G2D9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Histone-lysine N-methyltransferase SUV39H1 {ECO:0000256|ARBA:ARBA00040485};
DE EC=2.1.1.355 {ECO:0000256|ARBA:ARBA00012183};
DE AltName: Full=Suppressor of variegation 3-9 homolog 1 {ECO:0000256|ARBA:ARBA00041906};
DE Flags: Fragment;
GN ORFNames=N303_01744 {ECO:0000313|EMBL:KFO76088.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO76088.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO76088.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO76088.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC Evidence={ECO:0000256|ARBA:ARBA00036480};
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000256|ARBA:ARBA00004584}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KL447665; KFO76088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091G2D9; -.
DR STRING; 55661.A0A091G2D9; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0046974; F:histone H3K9 methyltransferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.40; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR011381; H3-K9_MeTrfase_SUV39H1/2-like.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR46223; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H; 1.
DR PANTHER; PTHR46223:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H1; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF009343; SUV39_SET; 1.
DR SMART; SM00468; PreSET; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Centromere {ECO:0000256|ARBA:ARBA00023328};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR009343-2};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KFO76088.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFO76088.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR009343-2}.
FT DOMAIN 1..35
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 121..182
FT /note="Pre-SET"
FT /evidence="ECO:0000259|PROSITE:PS50867"
FT DOMAIN 185..267
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR009343-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO76088.1"
FT NON_TER 267
FT /evidence="ECO:0000313|EMBL:KFO76088.1"
SQ SEQUENCE 267 AA; 29977 MW; 1FF21613389FB535 CRC64;
EEFYLVKWCG YPSSSNTWEP RKNLHCRGLL KQLHQDLERV PGGPARPGPR GLPARATSYL
VQKAKQRQAL RRWERLLNNT RSHRGRIVVE NEVDLHGPPS DFVYINEYKV GAGVNLVPVA
VGCECGDCLA NAVGGCCPGA SSNKFAYNEA GQVCIRAGLP IYECNSRCRC GADCPNRVVQ
KGIRYDLCIF RTGDGRGWGV RTLQRIRKNS FVMEYVGEII TSEEAERRGQ VYDRQGATYL
FDLDYVEDVY TVDAAHYGNI SHFVNHS
//