ID A0A118K5E9_CYNCS Unreviewed; 995 AA.
AC A0A118K5E9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 28-JUN-2023, entry version 33.
DE SubName: Full=CXC domain-containing protein {ECO:0000313|EMBL:KVI09000.1};
GN ORFNames=Ccrd_012623 {ECO:0000313|EMBL:KVI09000.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVI09000.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVI09000.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVI09000.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(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 -!- 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:KVI09000.1}.
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DR EMBL; LEKV01001075; KVI09000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A118K5E9; -.
DR STRING; 59895.A0A118K5E9; -.
DR EnsemblPlants; KVI09000; KVI09000; Ccrd_012623.
DR Gramene; KVI09000; KVI09000; Ccrd_012623.
DR OMA; NDQAHAY; -.
DR Proteomes; UP000243975; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0031519; C:PcG protein complex; IEA:InterPro.
DR GO; GO:0140951; F:histone H3K27 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd10519; SET_EZH; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR026489; CXC_dom.
DR InterPro; IPR045318; EZH1/2-like.
DR InterPro; IPR025778; Hist-Lys_N-MeTrfase_plant.
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:SF19; CXC DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR45747; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 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; PS51576; SAM_MT43_EZ; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000243975};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 330..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 739..838
FT /note="CXC"
FT /evidence="ECO:0000259|PROSITE:PS51633"
FT DOMAIN 853..961
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 995 AA; 112128 MW; C99595C7CD542405 CRC64;
MAMSSSKVHP HSTDAGRSES PDVPTYSNGL DLMHTNTALQ ESATTPEISL VIDSLKLKVD
ADRCAYIMKR MEENRNKLAE ITRTHHKLST ERRNLGIING DKVDNLLTRR QKEAIDMQSR
VDISFGSSSN SQEDEYASVI LLGSGIAVKN SVRPIHLPKV EKLPPYTTWI FMDRNQRMTE
DQSVVGRRRI YYDRNGGEAL ICSDSEEEII NDEEDKKEFV DSEDNIIRGC CLVALVKLEH
PILSLIYWPS ACLESLVKSR LVIVQSPAVS PFLALAYGEM KYHQHFIQAR HEALSSRQNV
IESFDFNSFL DKDLEAAQDS FDNLFCRRCL VSVIVICVMF LVLVLYFLQP LNLLFLLWQI
FDCKLHGCSQ DLIFPAEKLT WDGPDEESVP CGPHCYLQVQ KLEATPSMQL NTERTPALSS
DASGVLVSRG KSNGPSLRRR SKPCKNGSIA SNTQNVTESS DSETRPVHDV IPYHSPLPHK
NKRGGKSGTH QRNSKHVANH VVTAMKRTQR NVASDSDSVA SGSPGSRDRE FLSNSLKESK
EASSWSPKAK SSSMRRSRRK DSLVPDDHKS LQVQVPYPLV KKEDVSTCRK EVTDFKSWRT
LEKALFEKGL EMFGRNRLVH HFDDLVHEGS GLHISSFFSL GSLKMELVIF YYSLLCLIAR
NLLGGLKTCS EVFHVLKCYE NKPSSKGSDS TNSLGDGCRV DSNENMGLAQ RRRSRFLRRR
NRVRRLKYTS KSAAYHSMRK RISDKKDMPC RQYKPCGCQS ACGDDCSCLK NGTTCEKYCG
CPKTCKNRFR GCHCAKSQCG SRQCPCYAAN RECDPDVCRH CWISCGDGSL GTPGRKGDNY
ECKNMKLLLK QQQRVLLGRS DISGWGAFLK NTVPKHEYLG EYTGELISHY EADKRGKIYD
RENSSFLFNL NDQYVLDACR KGDKLKFANH SPVLMVAGDH RVGIFAKERI SAGEELFYDY
RYEPDQAPAW AKKPEDSGSK KEDAAPSSGR AKKLA
//
