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Database: UniProt
Entry: A0A136J7M9_9PEZI
LinkDB: A0A136J7M9_9PEZI
Original site: A0A136J7M9_9PEZI 
ID   A0A136J7M9_9PEZI        Unreviewed;      1022 AA.
AC   A0A136J7M9;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific {ECO:0000256|ARBA:ARBA00015839, ECO:0000256|PIRNR:PIRNR037104};
DE            EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182, ECO:0000256|PIRNR:PIRNR037104};
GN   ORFNames=Micbo1qcDRAFT_161115 {ECO:0000313|EMBL:KXJ93168.1};
OS   Microdochium bolleyi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX   NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ93168.1, ECO:0000313|Proteomes:UP000070501};
RN   [1] {ECO:0000313|Proteomes:UP000070501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG   DOE Joint Genome Institute;
RA   David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA   Barry K., Grigoriev I.V.;
RT   "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT   beachgrass.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalytic component of the COMPASS (Set1C) complex that
CC       specifically mono-, di- and trimethylates histone H3 to form
CC       H3K4me1/2/3, which subsequently plays a role in telomere length
CC       maintenance and transcription elongation regulation.
CC       {ECO:0000256|ARBA:ARBA00002789, ECO:0000256|PIRNR:PIRNR037104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC         COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC         Evidence={ECO:0000256|ARBA:ARBA00000944,
CC         ECO:0000256|PIRNR:PIRNR037104};
CC   -!- SUBUNIT: Component of the COMPASS (Set1C) complex.
CC       {ECO:0000256|ARBA:ARBA00011755, ECO:0000256|PIRNR:PIRNR037104}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037104}.
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DR   EMBL; KQ964248; KXJ93168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136J7M9; -.
DR   STRING; 196109.A0A136J7M9; -.
DR   InParanoid; A0A136J7M9; -.
DR   OrthoDB; 950362at2759; -.
DR   Proteomes; UP000070501; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR   GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd20072; SET_SET1; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR024657; COMPASS_Set1_N-SET.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR044570; Set1-like.
DR   InterPro; IPR017111; Set1_fungi.
DR   InterPro; IPR024636; SET_assoc.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   PANTHER; PTHR45814:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   Pfam; PF11764; N-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF11767; SET_assoc; 1.
DR   PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 2.
DR   SMART; SM01291; N-SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS51572; SAM_MT43_1; 1.
DR   PROSITE; PS50280; SET; 1.
PE   4: Predicted;
KW   Chromatin regulator {ECO:0000256|PIRNR:PIRNR037104};
KW   Chromosome {ECO:0000256|PIRNR:PIRNR037104};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR037104}; Nucleus {ECO:0000256|PIRNR:PIRNR037104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR037104};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037104}.
FT   DOMAIN          880..997
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1006..1022
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   REGION          131..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..690
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1022 AA;  116162 MW;  93B2B8A5F36B9A74 CRC64;
     MPKSRLRHTP YNVKPYQYDA ATSIGPGPPT QIVVSGFNPL LAFSKVTNTF ASFGEIAESS
     NKMHPNTGSY LGFATFRYRD SKRRTPFVSA IDAAKKAVRC MHGQRFEAKQ IVVQFDRDGK
     RSRRMLEHVL QKEEEAEKAR TPSIAPTPPM IPTGPRPRPS DASGRAAFLP PKGPAAERTP
     SISSIEPARA FPTKPKGYST IEPVVVSTTL KGEPYIFIAD SSVPVMPATI PHMKKRLKSF
     QFDDIRADRS GYYIIFPDTS YGRDEAFRCH RSANGSSFFT YTMAMKLCPG TKPDGLVETP
     QTTQRHAEPD KKPVIETRPQ DDQQKRQSER RRDEEAVLEE EKKQRAKNFD PVMEAVEAIR
     REMTEHLISH IRTKVAVPVL FDYLDPSNHV AKRRKLNLEN TAFPSRIAKT VEDREITPVS
     TPNSRADPIE RRTARLEVAA LPRIRKAKGQ HLAQRNAFTD PFARKRPATG RNAFRSLHYR
     LQSPDSDEDS DNEAEIRGSI VRDTEEPDSR PRSRMSTDED AFEDIFADED STTEAGSATP
     DRFGRTKKRK LDLQVEAAIK RQKKSDEELF GVTIDTLEHE FPSPVESTAV PSHDVQDDRT
     PEPIQLPTPT EKSTKLKKKP VPAKPKRKTK KQILEEEEEI QKRQQHEQQQ ETPVEEAQDR
     STEKEESMDE EPSKPKAIPE AKEEPVPVDD RFSDKVEPAW FLPKQWQLNI RTLGDLPFGA
     QDQPNLDRLK RKFKVAQIGD PKLWAWKHSR IHDLNAMDAS DDSPLRIEGY YVPNPTGCAR
     TEGVKKILNK EKSKYLPHHL KVQKAREERQ LKAARKDGKD AVTSATEAAR LAAEKLVAKG
     NSRANRVNNR RLVADLNDQK KTLGQDLDVL RFNQLKKRKK PVKFARSAIH NWGLYTMENI
     NKDDMIIEYV GEEVRQQIAE LRENRYLKSG IGSSYLFRID ENTVIDATKK GGIARFINHS
     CMPNCTAKII KVESTKRIVI YALRDIAQNE ELTYDYKFER EIGSLDRIPC LCGTTACKGF
     LN
//
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