ID A0A1D2NJB9_ORCCI Unreviewed; 961 AA.
AC A0A1D2NJB9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=Ocin01_01338 {ECO:0000313|EMBL:ODN05360.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN05360.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODN05360.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODN05360.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
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}.
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:ODN05360.1}.
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; LJIJ01000024; ODN05360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2NJB9; -.
DR STRING; 48709.A0A1D2NJB9; -.
DR OMA; YNYIPCD; -.
DR OrthoDB; 902834at2759; -.
DR Proteomes; UP000094527; 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 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; 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:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR Pfam; PF21358; Ezh2_MCSS; 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; 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:ODN05360.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000094527};
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:ODN05360.1}.
FT DOMAIN 718..820
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 827..942
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 22..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ODN05360.1"
FT NON_TER 961
FT /evidence="ECO:0000313|EMBL:ODN05360.1"
SQ SEQUENCE 961 AA; 108351 MW; AD3388E3C919F1C2 CRC64;
VTTFTTEEEE VLLSDLIWRK ESVTGSGVKG GTPSSSKREV GSNDKKSVEN ESSTTHSSSS
SRDKDRGSET PKNSTRGLDH GLEIPPFLMA TSVVRAAKAQ AVGKIAPSLM APVTSTTKSG
GKCSLTPELK RRIRSEYFRI LQQKRIRLKE DSKLAWIKNF NRTEGLMKEE NRKWKEARLS
NWEIDLDAPE HLGTMKRASL TLPMEHKSTH SVPIRIIHSI PSTPTMYMWS TIRQNVMVED
ETVLHNIPYM GEEVLDKDGN FIEELLKNYD GKVHTDKDHD YMDDECFMEM VRAVMAMEES
DIRNGLTKPH DKHSDTEEHF SDSEDDIHKG DSLLVKRMEP QQGMIINAEP GKVPRIKLPP
NRIFKLLSEV FPNNGTPAEL KEKYIELHEK HEPGAGLPPE CTPNIDGPTA ESVPREQTMH
SFHSLFCRRC YKYDCLLHRL KAYHPEPKML KRKCPEYRTK MPCSPFCFIN LPEVQARIEA
MASSTSDKDP DPVVNGEQGK VAPKKVRKQT SMESSGEQSS DDSNDSVAVL IGYRTSSCPK
SDGNNGNRRS GGGPAKQPPL ITDESKSDYV ENKGSKLKSS NSGGSSSSNN NPGEKLDFKE
NPAMNFAMQS YLHFQQFPES SNKPGVDTAA QSLIKDFQPQ DMDSWSGADQ SLFRAIHKVF
FHNYCLIAKS LATKTCQQVF YFAQKEAADM MTDGDSQKDV TPPPKKTKKK NRLWSLHCKK
IHMRKDPTSN SSVSNFTPCD HPGQPCDSSC SCIQAHNFCE KFCLCNSDCQ NRFPGCRCKA
QCNTKQCPCY LAVRECDPDL CQMCGADQYD KSKINCKNVS CQRGLYKHLL LAPSDVAGWG
IFLKDSAQKN EFISEYCGEV ITQDEADRRG KVYDKYMCSF LFNLNNEFVV DATRKGNKIR
FANHSVNPNC YAKVMMVNGD HRIGIFAKRA INPGEELFFD YRYGPTEQLK FVGIERESEF
L
//
