ID A0A364N636_9PLEO Unreviewed; 2297 AA.
AC A0A364N636;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific {ECO:0000256|ARBA:ARBA00015839};
DE EC=2.1.1.354 {ECO:0000256|ARBA:ARBA00012182};
DE EC=2.5.1.78 {ECO:0000256|ARBA:ARBA00012664};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|ARBA:ARBA00033302};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|ARBA:ARBA00029805};
DE AltName: Full=SET domain-containing protein 1 {ECO:0000256|ARBA:ARBA00030093};
GN ORFNames=DDE83_003878 {ECO:0000313|EMBL:RAR12730.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR12730.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) 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}.
CC -!- FUNCTION: Involved in amino sugar synthesis (formation of chitin,
CC supplies the amino sugars of asparagine-linked oligosaccharides of
CC glycoproteins). {ECO:0000256|ARBA:ARBA00003267}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-
CC ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2
CC H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;
CC Evidence={ECO:0000256|ARBA:ARBA00001697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001031};
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 -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC ribitylamino)uracil: step 1/2. {ECO:0000256|ARBA:ARBA00004917}.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC fructose 6-phosphate: step 1/1. {ECO:0000256|ARBA:ARBA00004775}.
CC -!- SUBUNIT: Component of the COMPASS (Set1C) complex.
CC {ECO:0000256|ARBA:ARBA00011755}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family.
CC {ECO:0000256|ARBA:ARBA00007424}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAR12730.1}.
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DR EMBL; QGDH01000046; RAR12730.1; -; Genomic_DNA.
DR STRING; 183478.A0A364N636; -.
DR UniPathway; UPA00113; UER00528.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000249619; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00714; GFAT; 1.
DR CDD; cd09209; Lumazine_synthase-I; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 3.40.50.960; Lumazine/riboflavin synthase; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR HAMAP; MF_00178; Lumazine_synth; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR047084; GFAT_N.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR034964; LS.
DR InterPro; IPR002180; LS/RS.
DR InterPro; IPR036467; LS/RS_sf.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR017111; Set1_fungi.
DR InterPro; IPR024636; SET_assoc.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR NCBIfam; TIGR00114; lumazine-synth; 1.
DR PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1.
DR Pfam; PF00885; DMRL_synthase; 2.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF11767; SET_assoc; 1.
DR Pfam; PF01380; SIS; 2.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF52121; Lumazine synthase; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51572; SAM_MT43_1; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS51464; SIS; 2.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:RAR12730.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000249619};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RAR12730.1}.
FT DOMAIN 116..417
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 489..628
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 660..801
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 1286..1376
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 2155..2272
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2281..2297
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1026..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1405..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1915..1937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1556..1583
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1026..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2297 AA; 254546 MW; FD1E50DFD1A3C700 CRC64;
MCLFDNNQRA AEASHYTPLI FLPVGLRHAG REKSAGKQQQ LKAVKGNVAS GTTLLSQRRG
GGCPGTATGT IGRSDVAQSD GTGFLKAGGS EGVPGHDEHC QSMVRVQGTR RHVANSGIFG
YINYLVEKDR KYILDTLINV LFAGLQRLEY RGYDSAGLAI DGDKKNEVYA VKEVGKVASL
KKLVEEQNFD LNKVFDSHAG IAHTRWATHG PPSRVNCHPH RSDANWEFSV VHNGIITNYK
ELKTLLESKG FKFETETDTE AIAKLTKYIY TEHPDLSFPA LVKAVIKELQ GAFGLLCKSV
HYPHEVVAAR KGSPLVIGVR TQKKMKVDFV DVEYNDEGAA LPAESASHNV ALKKSNNLLA
PPDKSLLHRS QSRAFLSDDG APMPTEFFLS SDPSSIVEHT KKVLYLEDDD IAHIHEGSLN
IHRLHKDDGS SNVRTIQTLE IQLQEIMKGQ FDHFMQKEIF EQPESVVNAM RGRLDPVNKT
VTLGGLRQYL STIRRCRRII FIACGTSYHS CMAVRGVFEE LTEIPIAVEL ASDFLDRQAP
VFRDDTCVFV SQSGETADSL GALRYCLERG ALTVGIVNNV GSSISLLTHC GVHINAGPEI
GVASTKAYTS QFVCMVMFAL SLSEDRASKQ KRREEIVEGL GKISEQFKEV LKLDQPIKKL
CERFKNQKSL LLLGRGSQHA TALEGALKIK EISYLHCEAV MSGELKHGVL ALVDENLPIV
MILTRDDIFA KSLNAYQQVI ARSGRPIIIC NVDDPEFPAD KTDKIEVPSN VDVLQGLINV
VPLQLMSYWM AVAEGVNVDM PRNLAKSVTV ESTLTLLLYT QTHQTKSSWH LSRVPARPRR
SALRIGIVHA RWNTKIIDAL LEGTKRKLKE AGVKDENIVV QSVPGSYELP YAVKQLYSAS
QIQSSNTGVV GAAADLLGST SDLTSLAGQS ATKTSNQPFD AIIAIGTLIK GETMHFEYIS
EAVSHGLMRL QLDNNVPVIF GLLTLLTDEQ GLMRAGIGGQ DGKSGHNHGE DWGSAAVELG
VKRRGFMSGR RRGENEDRSL RRAASHRAES PAPFHSALAA PVTAAGETRR LRHRKNSDSP
QNDAQRPSYL LDDVDSDSST PTPASSTFSA PPSMSRSGHN HSLHALTPLT SSDSSPPGKL
PSPRSSKLSH ETMHATSSST HTAPSSAPNN VADTITPINT PPETRRSVFP ADGVLGQRST
YDAQLDPKLD KRARAKGTAK YSTILDKGDP SPPPDPRLAI AGYTTGNYVI KTSFTGAPKS
KLRIAPYVAK PYSFDQRISC GPGPATQVVV TGFDPLTPDV QLRAFFSTYG EVETVRNQVH
PDNGSPLGIC LVKFRDTPPA RGTTGMKATT SAKRAEREGT NQRLAQQTIK VQSDREGRRC
KRLVDMAVQQ TRKEEEKLRA KFAAKTASSA TPATPGNFDL PANVPKGPSG KGARPPIPMP
REPLTRKAAL SFLIERDPIK PTLKRKPYIF LAHIYVPVLA TTIEHLKKRL KNFRWTSVRC
DPTGYYITFE ESKRGEEETV RCYKELHMQA LFTYTMNMEC NQYGDPNYER SPSPERVVAD
KKRKAIEERI EQEEAEDLEW EKKQRADSLD PVQAALDVLK QELQEKLLGD IKTKLAAPTI
LELLDPELHA EKRRRLNIPG PPKKDEDVRP PALLAPGFDA FGGNTPRGRN GGLGRGGRRG
LGAFDPSTRR GKKPPKIVNA FADERRKASA PKPRVARGLH RQMIEMFEPE ESDDESRSQL
TRGTEEQESR PISRAPSTDI EDEVEESSRA HRAKRRRIET GWGEDSDEEM DDSHARSLLA
HCIHKDPENM AEKELEQVLA ILPRSSPIWK KADKALKGFR RLRKIEQEAD AIFGVEVSPA
EKLEPEVVIT QDEEAQKPVE TTELAETLTS LKKKAAAKPK KKTKKQLQEE AKAAKAEAME
VETPVQEEEV PEAKEVKEVK EVVEEAVVED TAPGKDGRAS SVVWSVSHDI PRKTVEDDLS
VVMDIDGWQH LLKDEEDLRF LKAALASTTP ANIGDAQDWA WKQKSIKHLN RNGQEGISRT
ETKIEGYYVP NATGSARTEG VKKIRESEKS KYLPHRIRVQ KEREERQRRA KQEERSVVSV
EGFKFQTSAN KTSTANSRAN RANNRRMVND INISKNLSGA EGDALRFNQL KKRKKLVKFD
RSAIHNWGLY AQEPIAVNDM IIEYVGEKVR QRVADLREAK YDMQGVGSSY LFRIDEDTVI
DATKMGGIAR FINHSCTPNC TAKIIRVDNT KRIVIYALRD IQSDEELTYD YKFEREIDAT
DRIPCLCGSI GCKGFLN
//
