ID G8BJV0_CANPC Unreviewed; 810 AA.
AC G8BJV0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific {ECO:0000256|ARBA:ARBA00018028};
DE EC=2.1.1.359 {ECO:0000256|ARBA:ARBA00012178};
DE AltName: Full=SET domain-containing protein 2 {ECO:0000256|ARBA:ARBA00030091};
GN OrderedLocusNames=CPAR2_407180 {ECO:0000313|CGD:CAL0000149905,
GN ECO:0000313|EMBL:CCE44916.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE44916.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
CC -!- FUNCTION: Histone methyltransferase that trimethylates histone H3 'Lys-
CC 36' forming H3K36me3. Involved in transcription elongation as well as
CC in transcription repression. {ECO:0000256|ARBA:ARBA00003901}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC Evidence={ECO:0000256|ARBA:ARBA00000317};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; HE605208; CCE44916.1; -; Genomic_DNA.
DR AlphaFoldDB; G8BJV0; -.
DR STRING; 578454.G8BJV0; -.
DR EnsemblFungi; CPAR2_407180-T; CPAR2_407180-T-p1; CPAR2_407180.
DR CGD; CAL0000149905; CPAR2_407180.
DR VEuPathDB; FungiDB:CPAR2_407180; -.
DR eggNOG; KOG4442; Eukaryota.
DR Proteomes; UP000005221; Chromosome 4.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR GO; GO:0006354; P:DNA-templated transcription elongation; IEA:EnsemblFungi.
DR GO; GO:0006353; P:DNA-templated transcription termination; IEA:EnsemblFungi.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0060195; P:negative regulation of antisense RNA transcription; IEA:EnsemblFungi.
DR GO; GO:0045128; P:negative regulation of reciprocal meiotic recombination; IEA:EnsemblFungi.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:EnsemblFungi.
DR CDD; cd19172; SET_SETD2; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 1.10.1740.100; Set2, Rpb1 interacting domain; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR025788; Set2_fungi.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044437; SETD2/Set2_SET.
DR InterPro; IPR013257; SRI.
DR InterPro; IPR038190; SRI_sf.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR22884:SF413; HISTONE-LYSINE N-METHYLTRANSFERASE CG1716-RELATED; 1.
DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF08236; SRI; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF47676; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS51568; SAM_MT43_SET2_1; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005221};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 51..107
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 109..226
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 233..249
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 494..528
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 436..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..636
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 92175 MW; D5F4941967E2715E CRC64;
MNGNTSISKY APPLFLEVED KTEEALTKFH NLQISTYQSK SIAAPSSNKR AEYMTCDCEE
EWDGEQEMNL ACGEDSNCIN RLTSVECTNR HCLCGDDCQN QRFQKRQYAD VSVFQTELKG
YGLKANKPIS EGQFIYEYIG EVIDEGAFRQ RMIEYDMKNY KHFYFMMLKP DAFIDATEKG
SLARFVNHSC NPNAFVDKWV VGDKLRMGIF AKRNIAKGEE ITFDYNVDRY GAQSQPCYCG
EPNCIKFMGG KKQTDAALLL PEGIAEALGV TSKMEKAWLK ENKHLRGDQQ DDDSTINEIF
VQSLEIEPMD DVDVSKVMAA LLKSQQQSII AKLIMRMHMT DDPSVNSLMV KMHGYKTLSG
VLQGIEDEEL IKMVLEILSR WPAMTKNRIS SSQIEDVVKE IEANTTNEEI KQLASNLLSQ
WSVLEMTYRI PKTQKPDQSL MESYGRVSRS PEHRNGDTSG ATTFNQSDHG HYSNNASQMY
STSNTIAPVS NPDFGLPPNW RSQYDSNTQR YYYYNVLTNE TTWDKPGVSM PTRPKLPTGP
SNMVNQYSQV PYSNSHHSSP PPRNNNIEEE IARREEEKEK REREARAQEL TEKERKLREL
IEQAKTIKST PEPEKKSKHK HKHEHRSKHK HERSRPNPSG GKRAVAVAEQ DDEARVKHKS
SSHSHKKKEG KEVSLESQWK HVMAKHVPNL LKSYVDEIGK DNVKGCAKEI VNNLAAREAN
KGAPPSSSKE LDKHKLKKLK EYSDTYMEKF LTKYRSKHHG KRKLDEIEGE GETSATSPED
SKGVVDSSVS PSNTVTNGQG ENEDIKKVKL
//
