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Database: UniProt
Entry: A0A2H3SS26_FUSOX
LinkDB: A0A2H3SS26_FUSOX
Original site: A0A2H3SS26_FUSOX 
ID   A0A2H3SS26_FUSOX        Unreviewed;      1143 AA.
AC   A0A2H3SS26;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Related to polycomb group protein MEDEA {ECO:0000313|EMBL:SCO79268.1};
GN   ORFNames=BFJ69_g852 {ECO:0000313|EMBL:RKK86628.1}, FRV6_03481
GN   {ECO:0000313|EMBL:SCO79268.1};
OS   Fusarium oxysporum (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO79268.1, ECO:0000313|Proteomes:UP000219369};
RN   [1] {ECO:0000313|Proteomes:UP000219369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA   Guldener U.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SCO79268.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V64-1 {ECO:0000313|EMBL:SCO79268.1};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:RKK86628.1, ECO:0000313|Proteomes:UP000285084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo_A13 {ECO:0000313|EMBL:RKK86628.1,
RC   ECO:0000313|Proteomes:UP000285084};
RX   PubMed=30202022; DOI=10.1038/s41598-018-30335-7;
RA   Armitage A.D., Taylor A., Sobczyk M.K., Baxter L., Greenfield B.P.,
RA   Bates H.J., Wilson F., Jackson A.C., Ott S., Harrison R.J., Clarkson J.P.;
RT   "Characterisation of pathogen-specific regions and novel effector
RT   candidates in Fusarium oxysporum f. sp. cepae.";
RL   Sci. Rep. 8:13530-13530(2018).
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};
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DR   EMBL; MRCX01000004; RKK86628.1; -; Genomic_DNA.
DR   EMBL; FMJY01000002; SCO79268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3SS26; -.
DR   VEuPathDB; FungiDB:FOC1_g10016174; -.
DR   VEuPathDB; FungiDB:FOC4_g10014599; -.
DR   VEuPathDB; FungiDB:FOIG_01414; -.
DR   VEuPathDB; FungiDB:FOMG_01627; -.
DR   VEuPathDB; FungiDB:FOXG_17467; -.
DR   VEuPathDB; FungiDB:FOZG_01617; -.
DR   VEuPathDB; FungiDB:HZS61_001237; -.
DR   OrthoDB; 902834at2759; -.
DR   Proteomes; UP000219369; Unassembled WGS sequence.
DR   Proteomes; UP000285084; 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; IPR048360; Ezh2-like_CXC_fung.
DR   InterPro; IPR040968; Ezh2_MCSS_fung.
DR   InterPro; IPR040595; EZH2_N.
DR   InterPro; IPR041355; Pre-SET_CXC.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR45747; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR   PANTHER; PTHR45747:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE E(Z); 1.
DR   Pfam; PF21509; Ezh2-like__CXC_fung; 1.
DR   Pfam; PF18600; Ezh2_MCSS_fung; 1.
DR   Pfam; PF18601; EZH2_N; 1.
DR   Pfam; PF18264; preSET_CXC; 1.
DR   Pfam; PF00856; SET; 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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          605..722
FT                   /note="CXC"
FT                   /evidence="ECO:0000259|PROSITE:PS51633"
FT   DOMAIN          737..866
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          14..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          880..1054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1084..1143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..386
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..906
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        979..993
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1084..1098
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1143 AA;  128303 MW;  4AE309D7CCC62E4B CRC64;
     MASPHLVAIV AGKPDTIDLT GDSDSDYEPH SLVPLNRNNT TTARFTPNFS ISSERPSSTN
     APVSPPKLNR STSSIAASQD KQPSASAEPP RPASSVLKLS QKVTTITANS DDAQSMAKLS
     SVTASNLASR QVTPTPEKDA SKSTQQTKPA SPKYQTPKKQ EWDVAAIAEK LTQFRQDIKD
     GHSRMTSYII ESTKPNERRV LTGKNLFAGL TNKPVPSKKG ETMRIKSKEH TKLKNNKRED
     HYSIVRIQTD EERVPRYRFH HVEIKKNILT PNTMLTFVPH LRDLETSEEY KYNVWLQELE
     DIDRKSGFKP MSREEKVRIA VRSEFASTVL LYLGTWLDKL SLPGCNRSAL IRYMASREPD
     DAITPRQKSD ILNSHRPAES TTPPEANKAA NMFTEAFRRV FHQGQPPTKQ IELRDVLLLD
     ESVDSIMETK PTAKDGSSTQ HENEHDAVEY WLGTYSILGC LICFSHSCEH GEYDAQNCKR
     TLSILPRLSD TLKRRRRLPY SAADTVNGNG PLSPLCKRNC YRSSPRPVAA SIQRPWDEED
     HFILRSTVAT ADRSKVTKDP FCLVAQLLDR DCSDVFNEYQ KLNVSMSPVE PANRLQIRTV
     SWYDRFKKTL IGDWESHTKT HEHQKRELSE PCNHEGPCTS ESCICVQHGV LCEKFCGCTV
     ENCAYKFTGC ACHSQGKTCL SKGKERPCIC VQLNRECDPD VCGRCGVVER ADPENADNEV
     LHSTGCQNCS LQRGQAKSLA LGESQLEGVG YGLFTIEDIA QDDFIIEYVG ELITHDEGVR
     REARRGDVFD EESNISYVFT LLDNEGIWVD AATYGNLSRY INHASESDKR GCNITPRILY
     VNGEYRIKFT AMRDIKAGEE LFFNYGENFP NLTKKLLDHK VGGKSDQGKK RSRRPNGEGV
     ARKNPKTDKK KPGKGKKRAQ AVLDEDDMLA DTLGFAPKPL RKRKKGPFEE DSEEEEYHPT
     GTDASIMETP SDGDSDFGNS AARLRKRARQ DGKGAASSHN GKPRGDLKTR GKRGGARPGS
     GRPRKYPRKL TSAPMLEHPS ASESQDREDP EERQIVAADT IVPAALQRPQ PVEINDSMEY
     ITFSEERTEE SRLLQSQLEE DNDEDDDDDD QDVVVRSRVD RGVRNRRPTA KLRDDGDWIS
     GSQ
//
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