ID A0A1L7XVU5_9HELO Unreviewed; 1281 AA.
AC A0A1L7XVU5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=PAC_19061 {ECO:0000313|EMBL:CZR69161.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR69161.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR69161.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR69161.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-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}.
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; FJOG01000066; CZR69161.1; -; Genomic_DNA.
DR STRING; 576137.A0A1L7XVU5; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000184330; 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:UP000184330};
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 1139..1256
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1265..1281
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1281 AA; 142392 MW; C8F3323FC9BC5D3A CRC64;
MSRASGASFA QFFPSAPRAA KDKAKEREKY KSQGVDSPSI RPVADTKVSI PFSRADVPAL
SRPGGEIKPP INGFAAPAED NESQQGDLLN GVGSASSHTS TVSSGFSAPA QQSNMSTLGG
PRNVSSLTPL TNIESSPLST ASPQHKSGFH TINSNQLNNA IAVGTNSALP TQPPAEAPKP
TDTRVYARDP NKGLKGERCT YDPLLDKHDK HAAKRAKAIY KKFGWEDDAP PPDPRLSKPG
GKLDYINVDF HHPQSRLRQA PYLIKPYPYD PKTSLGPGPP TQVVVTGFDP LHNFANVAAI
FSSYGEVAES SNKLHPETGS CLGFATFRYR DSKRNHAGRI VTAIEAAKTA VRKGAGMRLG
TYNVKVEFDP EGNKSRRMME NVLKTSQVTP APQISKPAAT APKPAEKTSG PPPTAPKGPA
SSRPIFRPPL NPAVISAKPI QPVQPVRQRY VESAEPVSLQ LPHTPYLFVS GESVPVMPTT
PPHMLKRTRH FEADDVKMDK YGYYIVFPNN STGRYNCERC YHGLHGTLMF NYTMMIKMYL
WGTNGRSNTH RPSDATHNRS RSPPRHQIED RDKKDAEERR REEEADLEDE KKERAKNFDP
AREAIEVIRK ELKDQLVRNI RTKIAAPILH KFMDPSNHAA KRRKLNIPDP KDAKITIIHE
DDDREDSPAV GTPNSRADGE RPPMGAGRLN VAALPRIRKK EKGSKKENVG FKDPFGRVRP
GSSSRTVYRP LAHRFIHSED EDSDDDTESH SRARDTEEPD SRPRSRMTSE ESGDEPDVLR
RDLAKDDVAS VDTRDEDSMS EANFVVGEPI KQRPMKRKLD LQVEAAIKRQ KKKTDEELFG
VAQDKIEEQF PLSASTVDDD NPMDIDAIVK TEGGAEAAFA AGKKKVATKQ KKKSKRQIFE
EREALKRQQE GIYMEEALRQ ASEAIEDDEE DVIIETAPVE TTVEWGMSGE SPRPTVDDDF
ANLLDLDGLQ NLLKDEEDAP LAIDTFNDPT SAGEGYSTAW AWKQEDIKGL NRSGYRGLVT
EPTEVHGYYV PNETGCARTE GTKKILNSEK SKYLPHRIKV QKQREEMQAE ASKSGKSAIV
QAQEAARVAA EKQAAKGNSR ASRVNNRRFM ADVNDQRKNL NLGNDTDALR FNQLQKRKKP
VKFARSAIHN WGLYAMENIA MNDMIIEYVG EKVRQQVADF REHSYLRSGI GSSYLFRIDE
STVVDATKKG GIARFINHSC LPNCTAKIIT VEKSKRIVIY ALRDIAQNEE LTYDYKFERE
IGSTDRIPCL CGTAACKGFL N
//
