ID A0A091HQU7_CALAN Unreviewed; 729 AA.
AC A0A091HQU7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=[histone H3]-lysine(27) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012186};
DE EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
DE Flags: Fragment;
GN ORFNames=N300_06177 {ECO:0000313|EMBL:KFO97549.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO97549.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFO97549.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO97549.1};
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(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-
CC COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356;
CC Evidence={ECO:0000256|ARBA:ARBA00000090};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KL217652; KFO97549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HQU7; -.
DR STRING; 9244.A0A091HQU7; -.
DR Proteomes; UP000054308; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00167; SANT; 1.
DR CDD; cd19217; SET_EZH1; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR026489; CXC_dom.
DR InterPro; IPR045318; EZH1/2-like.
DR InterPro; IPR048358; EZH1/2_MCSS.
DR InterPro; IPR021654; EZH1/EZH2.
DR InterPro; IPR044438; EZH1_SET.
DR InterPro; IPR041343; PRC2_HTH_1.
DR InterPro; IPR041355; Pre-SET_CXC.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR PANTHER; PTHR45747; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR PANTHER; PTHR45747:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EZH1; 1.
DR Pfam; PF21358; Ezh2_MCSS; 1.
DR Pfam; PF11616; EZH2_WD-Binding; 1.
DR Pfam; PF18118; PRC2_HTH_1; 1.
DR Pfam; PF18264; preSET_CXC; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01114; CXC; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51633; CXC; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KFO97549.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054308};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
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, ECO:0000313|EMBL:KFO97549.1}.
FT DOMAIN 487..589
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 596..711
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 169..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO97549.1"
FT NON_TER 729
FT /evidence="ECO:0000313|EMBL:KFO97549.1"
SQ SEQUENCE 729 AA; 83610 MW; DC87CC01410439FC CRC64;
WKRKVKSEYM RLRQLKRFQA NMGAKALFVA NFAKVHEKTQ ILNEDWKKLR VQPVQLMKPV
SGHPFLKQCT VESIFPGFPS QTLYMRTLNT VALVPIMYSW SPLQQNFMVE DETVLCNIPY
MGDEVKEEDE TFIEELINNY DGKVHGEEGS VLISDAVFLE LVNALNQYSD EEEEGHNDSE
VKQEDGKEEL PVTKKRKRIA VEGNKKCSKK RFPNDMIFTA ISSMFPEYGF PEDMKERYRE
LTEVSDPNVL PPQCTPNIDG PCAKSVQREQ SLHSFHTLFC RRCFKYDCFL HPFHATPNVY
KRKNRETKIE PDPCGADCFL WLEGAKEFAA LHNPRSKCSG RRRRRHHVVG ASCSSAPTSA
VTETREGDSD RDTGNEWASS SSEANSRCQT PTKQKQSPAS SQLFAVETPQ EPVEWTGAEE
SLFRVFHGTY FNNFCSIARL LGTKTCRQVF QFAVKESLIT KLPTNELMNP SQKKKRKHRQ
VLWAAHCRKI QLKKDNSPTQ VYNYQPCDHP EHPCDSSCPC IMTQNFCEKF CQCNPDCQNR
FPGCRCKTQC NTKQCPCYLA VRECDPDLCL TCGASEHWDC KVVSCKNCSI QRGLKKHLLL
APSDVAGWGT FIKESVQKNE FISEYCGELI SQDEADRRGK VYDKYMSSFL FNLNNDFVVD
ATRKGNKIRF ANHSVNPNCY AKVVMVNGDH RIGIFAKRAI QAGEELFFDY RYSQADALKY
VGIERETDI
//
