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
//