ID A0A3R7ILN0_9STRA Unreviewed; 1054 AA.
AC A0A3R7ILN0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU271113, ECO:0000256|RuleBase:RU362120};
DE Includes:
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|RuleBase:RU271113};
DE EC=2.1.1.360 {ECO:0000256|RuleBase:RU271113};
DE AltName: Full=Histone H3-K79 methyltransferase {ECO:0000256|RuleBase:RU271113};
DE Includes:
DE RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000256|RuleBase:RU362120};
DE EC=1.1.1.49 {ECO:0000256|RuleBase:RU362120};
GN ORFNames=BBI17_007193 {ECO:0000313|EMBL:RLN32443.1}, BBO99_00007237
GN {ECO:0000313|EMBL:RLN76835.1}, JM16_006779
GN {ECO:0000313|EMBL:KAG2520283.1}, JM18_006687
GN {ECO:0000313|EMBL:KAG2521219.1};
OS Phytophthora kernoviae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN32443.1, ECO:0000313|Proteomes:UP000285883};
RN [1] {ECO:0000313|EMBL:KAG2520283.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2520283.1}, and NZFS 3630
RC {ECO:0000313|EMBL:KAG2521219.1};
RX PubMed=26981359;
RA Studholme D.J., McDougal R.L., Sambles C., Hansen E., Hardy G., Grant M.,
RA Ganley R.J., Williams N.M.;
RT "Genome sequences of six Phytophthora species associated with forests in
RT New Zealand.";
RL Genom Data 7:54-56(2015).
RN [2] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chile2 {ECO:0000313|EMBL:RLN32443.1}, and Chile4
RC {ECO:0000313|EMBL:RLN76835.1};
RA Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA Williams N.M., Mcdougal R.L.;
RT "Genome sequencing of oomycete isolates from Chile give support for New
RT Zealand origin for Phytophthora kernoviae and make available the first
RT Nothophytophthora sp. genome.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2520283.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2520283.1}, and NZFS 3630
RC {ECO:0000313|EMBL:KAG2521219.1};
RA Studholme D.J.;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC phosphate pathway, which represents a route for the dissimilation of
CC carbohydrates besides glycolysis. {ECO:0000256|RuleBase:RU362120}.
CC -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC histone H3 to form H3K79me3. This methylation is required for telomere
CC silencing and for the pachytene checkpoint during the meiotic cell
CC cycle by allowing the recruitment of RAD9 to double strand breaks.
CC Nucleosomes are preferred as substrate compared to free histone.
CC {ECO:0000256|RuleBase:RU271113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:61548; EC=1.1.1.49;
CC Evidence={ECO:0000256|RuleBase:RU362120};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60328, Rhea:RHEA-COMP:15549, Rhea:RHEA-
CC COMP:15552, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.360;
CC Evidence={ECO:0000256|RuleBase:RU271113};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 1/3. {ECO:0000256|ARBA:ARBA00004937, ECO:0000256|RuleBase:RU362120}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU271113}.
CC -!- MISCELLANEOUS: In contrast to other lysine histone methyltransferases,
CC it does not contain a SET domain, suggesting the existence of another
CC mechanism for methylation of lysine residues of histones.
CC {ECO:0000256|RuleBase:RU271113}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. DOT1 family. {ECO:0000256|RuleBase:RU271113}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009975, ECO:0000256|RuleBase:RU362120}.
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:RLN32443.1}.
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DR EMBL; JPWV03000246; KAG2520283.1; -; Genomic_DNA.
DR EMBL; JPWU03000257; KAG2521219.1; -; Genomic_DNA.
DR EMBL; MAYM02000825; RLN32443.1; -; Genomic_DNA.
DR EMBL; MBDN02000287; RLN76835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7ILN0; -.
DR STRING; 325452.A0A3R7ILN0; -.
DR UniPathway; UPA00115; UER00408.
DR Proteomes; UP000285624; Unassembled WGS sequence.
DR Proteomes; UP000285883; Unassembled WGS sequence.
DR Proteomes; UP000785171; Unassembled WGS sequence.
DR Proteomes; UP000792063; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00966; G6PD; 1.
DR InterPro; IPR025789; DOT1_dom.
DR InterPro; IPR001282; G6P_DH.
DR InterPro; IPR019796; G6P_DH_AS.
DR InterPro; IPR022675; G6P_DH_C.
DR InterPro; IPR022674; G6P_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00871; zwf; 1.
DR PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR Pfam; PF08123; DOT1; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51569; DOT1; 1.
DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU362120};
KW Chromatin regulator {ECO:0000256|RuleBase:RU271113};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526,
KW ECO:0000256|RuleBase:RU362120};
KW Methyltransferase {ECO:0000256|RuleBase:RU271113};
KW NADP {ECO:0000256|RuleBase:RU362120};
KW Nucleus {ECO:0000256|RuleBase:RU271113};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU362120};
KW Reference proteome {ECO:0000313|Proteomes:UP000285624};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU271113};
KW Transferase {ECO:0000256|RuleBase:RU271113}.
FT DOMAIN 690..1015
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 509..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ SEQUENCE 1054 AA; 118475 MW; D165CA310AE7CD55 CRC64;
MSLSNSNSNE QLPTVDEHHA CEYLGTALTI FVIGASGDLA KKKTYPSLFA LYVMGYLPEH
VVIVGYARSP KNDVDFRAQI APWIKPKNSE YEAKKEAFLN KLIYRSGAYD SAEDVGKVSK
EMEALEEAKG SSVINRLFYF AIPPSVFVPI GTSIKKAALT TRGWNRLIVE KPFGHDLSSF
NKLSADMGAL YGEDEIYRID HYLGKEMVQN LLILRFANAI YEPIWNRNYI SSVTITFKED
IGTQGRGGYF DSYGIIRDVM QNHLLQVLSL VAMEPPARAA GKDYSNYIRD EKVKVLNCIE
PIKLENTVLG QYQGDKERNE PGYLEDPTVP KGSVTPTFAT TVMYVNNPRW AGVPFIMKAG
KALNERKGEI RVQFKAPPGA EHMFPGVKIP VQELVMRLQP DEAVYIKMNV KSPGLQTKAI
SSELDLSYAE RYEGAEVPDA YTRLILDVLR GKQAAFVRDD ELRAAWTIFT PLLDEIEGQK
VKPLPYAFGS RGPKESDELV NKVGFQYHHA NRKGPRSAEH RKFKRPHELS PGAVVSTSFE
AFDAKPTTYT WNTSQGTDDA LPPVINEEIA ANETSTTAEE SVNKLETMDA SDVASSVPSS
PRATASSSSD GETTALLQHA QQLQRKKDTM KSIKEDQEQE EQELRRSRRK RRPVELLSPS
EELPHSKSPN KRRIISAKNE MVEILIRARP AVQVTAVARA AAAKKEEKKK RTQPLVKRKK
NTPKKEKETR VILSPVQDEK KKTPLKKRSS KARRSLEPAY SYESQTEYVS NLIAELYEEQ
EQDDRGMYNI SRDTVVTETS TCKRSQEVQD LSMEEFRRLM TYGEVSVESV SSTILPFLRL
GEEDVFFDLG CGTGKILVQA ALQTPCKTTI GIELMQNRVQ EGEKALARLE ERDIPILRGK
RIEVLQGDIC EPPDEAGLMN ATVVFINNVM FGPVLMLKVM ALLKDMRKLK RVVMLRKICE
RHGNEKCTRA GNYCIDYVHP PEEAEIDVSW ADKTSVYLYE SLEYSLGELR RQMINMQSPT
VQSPTPKGKG KKQSSHVPPV SHADFEAKLD AVAS
//
