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Database: UniProt
Entry: A0A1V9XBZ1_9ACAR
LinkDB: A0A1V9XBZ1_9ACAR
Original site: A0A1V9XBZ1_9ACAR 
ID   A0A1V9XBZ1_9ACAR        Unreviewed;       789 AA.
AC   A0A1V9XBZ1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=[histone H3]-lysine(27) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012186};
DE            EC=2.1.1.356 {ECO:0000256|ARBA:ARBA00012186};
GN   ORFNames=BIW11_01575 {ECO:0000313|EMBL:OQR71039.1};
OS   Tropilaelaps mercedesae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC   Tropilaelaps.
OX   NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR71039.1, ECO:0000313|Proteomes:UP000192247};
RN   [1] {ECO:0000313|EMBL:OQR71039.1, ECO:0000313|Proteomes:UP000192247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR71039.1};
RX   PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA   Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT   "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT   is shaped by the parasitic life history.";
RL   Gigascience 6:1-17(2017).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQR71039.1}.
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DR   EMBL; MNPL01015526; OQR71039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9XBZ1; -.
DR   STRING; 418985.A0A1V9XBZ1; -.
DR   InParanoid; A0A1V9XBZ1; -.
DR   OrthoDB; 902834at2759; -.
DR   Proteomes; UP000192247; Unassembled WGS sequence.
DR   GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR041355; Pre-SET_CXC.
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:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR   Pfam; PF21358; Ezh2_MCSS; 1.
DR   Pfam; PF18264; preSET_CXC; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM01114; CXC; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:OQR71039.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OQR71039.1}.
FT   DOMAIN          547..648
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          655..770
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   789 AA;  88587 MW;  94DDB0B557E1D080 CRC64;
     MEGRASRSQT NAAEREAKEA KGGSTVITRS ERKDAEAARV EIPGRIRRRV EQEYVKIRNA
     HKEKRTRQII EKYSDNRRYV RETLEATRAS RKYGVKPQSV FPEMPAQGKL VKKVSVEVYS
     GGSGGSSVRQ AVPCKLMTAV QAIPTMYTWA PTQQNFLVED ETVLHNIPYM GDDQDDSFIE
     ELINNYDGKI HGDNDRKNTV NDERLIELVN ALMKYEDVAT MYTQKELEDN LSDPPEYLFA
     CVHAVFPSLA GSPHDLLEKY RQLTGKGPKV PVGQCTPNID GPVALSVPRE QSMHSFKALF
     CRRCYKYDCF LHSQGSVPQH KRRYYDMKVD SEPCGDKCYL HLSHVKEERA KEAKEAEEAK
     EAREAREHQW DLAGGSEAAP GLIGADGTFL EGAIKIESRN LEQGITPGTA ALAHHPDSGN
     EGSDDSNDAH IARDGLGQTR QKVTVNSLAT ESERAKQAPS SPQSELSARE SSEVWSAAEQ
     SLFRVLSKPF YKNFCAMAAI MVTKTCAQVY TFAQNEPVDV APPPEDTDDD SRRAKKKKKH
     KMWSTHSRKF AVKNAAGPGL ACQYSPCHHP GQPCDTTCPC VQLRNFCEKF CHCSPDCLHR
     FPGCRCKAQC NTKQCPCYLA VRECDPDLCQ ACGADQLQVS NITCKNVCLQ RGLRKHLLMA
     PSDIAGWGIF LKDAAAKNEF ISEYCGEIIS QDEADRRGKV YDKYMCSFLF NLNSDYVVDA
     TRKGNKIRFA NHSIQPNCYA KVLMVNGDHR IGIFANRNIL PGEELFFDYR YGPTEQLKFV
     GIEREIEYL
//
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