SET1_COCIM
ID SET1_COCIM Reviewed; 1271 AA.
AC Q1DR06; J3K3Q9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
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; ORFNames=CIMG_07257;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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}.
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DR EMBL; GG704912; EAS31778.3; -; Genomic_DNA.
DR RefSeq; XP_001243361.1; XM_001243360.2.
DR AlphaFoldDB; Q1DR06; -.
DR SMR; Q1DR06; -.
DR STRING; 246410.Q1DR06; -.
DR PRIDE; Q1DR06; -.
DR EnsemblFungi; EAS31778; EAS31778; CIMG_07257.
DR GeneID; 4562336; -.
DR KEGG; cim:CIMG_07257; -.
DR VEuPathDB; FungiDB:CIMG_07257; -.
DR InParanoid; Q1DR06; -.
DR OMA; CHMTALF; -.
DR OrthoDB; 1017537at2759; -.
DR Proteomes; UP000001261; 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: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; IPR017111; Set1_fungi.
DR InterPro; IPR024636; SET_assoc.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45814; PTHR45814; 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; 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; PS51572; SAM_MT43_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1271
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000269770"
FT DOMAIN 1129..1246
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1255..1271
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1271 AA; 141606 MW; DB6F21921726D001 CRC64;
MSRAPAGFAD FFPTAPSVLQ KKRSKAAQDR HAANTPKAAD PLPNLGLSST PDIKGGVGTS
ADNPVRAVGE RSAETTLALG DTNGATSSSS LSTGSSGFFS ASAPPGVAKP NGISSCALTP
LTNTDSSPPC KIESPLGSKS GSTDAAPQLA PTCEAHGGPE PVTITPLHTP PTPRVQARPA
NSEVKGHKIT YDPDLDRKFP SKARRRKPQY ETFGVDDEKD PPPCDPRMAI ANYTRGAACK
QKTKYRPTPY ILRPWAYDPT TSVGPGPPTQ IVVTGFDPLT PIAAISALFS SFGDIGEINN
RTDPMTGRFL GVCSIKYKDS RAFRGGISLS ASQAVRRAYL ECKKEQRIGT RRIRVELDRN
GVVSGRMVAK LITAQKAEFP SLEESRKESV GDNDNRLPIG DGAKKDNEQS KDNLPPSTAP
KGPSGRSSLH PSLLAPDGPR AVLKSPVPSR IEETPILQQI KRDPYIFIAH CYVPVLSTTV
PHLERRLKLY DWKAVRCDKT GYYIIFENSR RGELEAERCY RMCHMTALFT YVMNMECQPY
GNPNYERSPS PERIKAEKRE KAKRERLHRE MELDIEEEKR LRVENLDPAR EALSVLIIEL
RDKLLDDVKS RVAAPALYDF LEPDRHNAKR QQLGIPAPEG TGRPSFRIDA STDGTVVHSQ
PDAYSRHHRP GGVSSLNVLA LPRIRKVKGF EQGNAVYIDE RRRAKPRKRE FRPLYHRLQQ
LHEIEDSDDD QQVSFARDTE EVESRPLSRL SSESAESDNE DDLMRKSPSL LDAKPLDVPL
PESESLAGGI EQSGLPDREK SIIEELERGI NTLPTSSKKR KRLIEELATR KKRKEVDNLF
ELDAKPLESL VEETAQEALP ADSTDALRTV TPVLKDKKRK VKGQSGKQIF EERQAPKRKE
IDSTQPLLFE ESVELLPEGE IEISEPAIEE LKPEVEWGVS TDEPRPTAED DDTIVLDLDG
WQSLIKDDED INFLKKALSE HLAADIGNLA AWTWKHKEIK AINRGGDRGP VHSETRIDGY
YVPNPSGSAR TEGRKRIRES EKSKYLPHRI KVQKAREERL AKAKNDPHAA AAEAARLLAA
KSLSKSTSRS TRVNNRRLIA DINAQKQALP MQNGDSDVLR FNQLKKRKKP VRFARSAIHN
WGLYAEENIS ANDMIIEYVG EKVRQQVADM RERRYLKSGI GSSYLFRIDE NTVIDATKRG
GIARFINHSC TPNCTAKIIK VDGSKRIVIY ALRDIDRDEE LTYDYKFERE WDSDDRIPCL
CGSAGCKGFL N
