SET1_CRYNB
ID SET1_CRYNB Reviewed; 1469 AA.
AC P0CO27; Q55U33; Q5KIA9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9Y7R4};
DE AltName: Full=COMPASS component SET1;
DE AltName: Full=SET domain-containing protein 1;
GN Name=SET1; OrderedLocusNames=CNBD2720;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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:0000250|UniProtKB:Q9Y7R4}.
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:0000250|UniProtKB:Q9Y7R4};
CC -!- SUBUNIT: Component of the COMPASS (Set1C) complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL21216.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAEY01000020; EAL21216.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_775863.1; XM_770770.1.
DR AlphaFoldDB; P0CO27; -.
DR SMR; P0CO27; -.
DR EnsemblFungi; EAL21216; EAL21216; CNBD2720.
DR GeneID; 4935661; -.
DR KEGG; cnb:CNBD2720; -.
DR HOGENOM; CLU_004389_0_0_1; -.
DR Proteomes; UP000001435; Chromosome 4.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IEA:InterPro.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.70.330; -; 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; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45814; PTHR45814; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1469
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000410118"
FT DOMAIN 1327..1444
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1453..1469
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1469 AA; 163056 MW; 046DE4E651BCCCB3 CRC64;
MAPHEKGVNP SESPSGSLKK APPSGPKALR GFASPSAFRN AGIGNGLLQH RGEDERISFA
FPRKGKESLD RNGERPAPMS LESRLGPPVS RFNRPVGGDS LERGNGKGGW DNRDERTSAS
SSSIHRINKE KIRPRSDFIE SSANLYSEDD RNRDRGRYHE RDRSRGTNGD RGGGEGHSHR
EPGRGKEHQN GQGRDRSLYR DHSRERESSR DERDRYSEEY KHQRSKARFS PSPSPERSRL
KSSLGRHRSP VSVSSSSSSS ARSPPPVQNR EPLRYNGSQS KNGEKELSNG LLENSISRSG
VSIAVPRKLE TKQLVRPSPP HVNLKSTIQD NPSPPTGKYP PSPPSLDILS KPSCNREPLP
DQRPPTPPLP ENSSPTSPSL ESSRFDQNQH LLPDELPLPP LSISFPQKPV SSSSLSRLSS
LSAALSRPNP LDKDGTSMPP SFHFREISNR HQRLSPPNNA ENQLPETSII PPPPSETVPE
PPWIRPPYIP PPCTKHRPGI GNFFITNLRE KVEDKSGKEE KRVDGMEGGK VVQVTDPRLS
MTEEQRGRGR GSSKQRAAFY ELTYEWDLYS VTPKPPSPPT AVLITGLGPL TTVDQITKFL
RPHGRIKEID SKVDRKTDMQ LGICWVKFEG PPLGRPGTAH DVASMAVKVC DGKKISMGGE
RIRVVLDGRG KRAEQAVKEE MERRYPPKKP SALPSDMKVT PLSGTAMATT SRPPNAPNAS
TPLIDKQTFD TSAKAPIIRP GVLKPLGQKM YHRPSAPPLV FNNHRFRDES FLNRPFNAGA
GMISQQQMGY KILPGKPVQQ LASSFTSAPF VRHPRERRED SWTNERGRRL KGESSTRHWR
ARSLSRSSYS SYSSYSSYSE ESEEERPRHP TKVPYPQRKR LATGPSKEDE YKMEDVREAI
RENGHPCVFI DAKSLPAARE YESRQSHLGW YILFADDTTA YRVQRVLDTT AVQGHRLSLV
VHTSSGPRAQ TDASEPVTGG VGESKKGNWR YLTITKKSRP MPAVKKSGKS ATIRRKVYSP
SVSGSDDDDE QVPVMAQNRK RAPSYASSTS PLSEDDRPFA RSVQREERDI DKEGKFSLIG
KKADVVSVKA AKGPKSKTIR VDSDEVEENQ GVPLASIGEV TKAEGKQDDS TVVKLETLLS
ESISELTKGK KRPTKAKGGK ATKKVRLDQE ADDAATKIQI DEDIVPQPPK KKKVVKTEVD
KLLASGVLMD EEDAYWLGRV LAAQEDGLEP IWSDGEEDLV DEGHPLFHKS GAWRAEGWKK
VAQVQKSRYL PQRNRAVVNS EDVGGITTGR TARLAGRDQH RQTAAVAANN TVESDLFAFN
QLRIRKKQLR FARSAIEGYG LYAMETIHAG EMVCEYVGDL VRATVADVRE QRYLKQGIGS
SYLFRIDNDI VCDATFKGSV SRLINHSCDP SANAKIIKVN GQSKIVIYAE RTLYPGEEIL
YDYKFPLESD PALRVPCLCG AATCRGWLN
