ID X0HTA3_FUSOX Unreviewed; 1258 AA.
AC X0HTA3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=FOPG_06480 {ECO:0000313|EMBL:EXL79707.1};
OS Fusarium oxysporum f. sp. conglutinans race 2 54008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089457 {ECO:0000313|EMBL:EXL79707.1};
RN [1] {ECO:0000313|EMBL:EXL79707.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54008 {ECO:0000313|EMBL:EXL79707.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW808.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXL79707.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=54008 {ECO:0000313|EMBL:EXL79707.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Annotation of Fusarium oxysporum PHW808.";
RL Submitted (MAY-2012) 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; JH658831; EXL79707.1; -; Genomic_DNA.
DR AlphaFoldDB; X0HTA3; -.
DR Proteomes; UP000030676; 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: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; 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; 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 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 1116..1233
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1242..1258
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 140203 MW; 1E49B4AE483799B1 CRC64;
MTRPPGASFA QFFPTAPKVK AQSQTRPDLN RDREQSKPGS TPVSMTGACD PTSTSAASDA
DANAGQNGIV SASDTMPAQP DDTESPFTDI PSTVDSASSY SSTASSIFST TARHGAAATS
ASSRLPTSSL TPIASKDSPN SLASATTKPD MSTCLTADRA ARQSSRNSPA VGFNGSISNG
LPSNERIPAR DPMPSVKGLK CTYDPLLDRV HNKSVSKNAK PTYKEFGRDD DAPPKDPRLA
KSDGRLGYIN TDYYLPKSRL RTAPENIKPY PYDPKTSIGP GPPTQIVVTR YNPLVPFSKV
TAIFATFGEI AESSNKMHPE TGSYLGFATI RYRDSKRPDR PPVSAIDAAR RAVRTRGIKV
DADIVRVEYD AEGRRSRRML EEHLKREKEK FEKKEQERLA LAAKAPPTGP KSGTAPGFTR
PPPTAPKGPS AQRQPVVPGA PQLSLPPSQQ KGLNLESSNL TQKLADDPYI YVTGDSVPVL
PSILPHMKKR LKNYGFEEIR VDKSGYFIVF RNSFTGKSEA ERCFRAVNHT EFFNYDMTMQ
LCLPRPRRDG ASGHRRSSAS PERKTNTEPR YRDEKERRRR EEEADFEEEK KQRAKNFDPV
IEAVEVVRRE MTEHLIRHIR TKVAAPALSD FLDPANHAAK RRKLNIEHPD DLQDMASIED
GNDSSRVGTP NSRADPIERR TGRIEPKALP RIRKTKVKQK NAFVDPFARK RPPVARNAFR
SLHHRLRSLD SDVESDDDTD TRTLLARETE EAESRPRSRM STDDEASKDD FVPWEQGEDD
SMTEASFAIA DSAISRKRKL AESVESAFKR QKKSDEELFG VRLRALGSGF ETREDSVDII
PEPETGDDID SRISRSETPV SVVGKPLKKR PSRAKKTKIF EELEAQDLQT ETDSQRDEEE
AVEPPNAKKT GADTEKSTTK EDVTEKYDEK LLSTEPLTPA LALPDGAKPD LPLFQGLAIG
QSDIPDLSKL SRRFTAKDIG NPELWLWTRN RIRELNSASR TLDSPVTISG YYVPNPTGCA
RTEGVKKILN SEKSKYLPHH IKVQKARQER EARNKSGKDA AADAARIAIE KQAANDSERQ
KRATNRRYVQ DLNDQKKTLG QDSDIFKFNQ LKKRKKPVKF ARSAIHNWGL YAMENIAKDD
MIIEYVGEQV RQQIAEIREN RYLKSGIGSS YLFRIDDNTV IDATKKGGIA RFINHSCEPN
CTAKIIKVEG SKRIVIYALQ DIAMSEELTY DYKFEREIGS LDRIPCLCGT AACKGFLN
//
