SET2_COCIM
ID SET2_COCIM Reviewed; 1011 AA.
AC Q1DU03; J3K868;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 specific;
DE EC=2.1.1.359 {ECO:0000250|UniProtKB:P46995};
DE AltName: Full=SET domain-containing protein 2;
GN Name=SET2; ORFNames=CIMG_06210;
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: Histone methyltransferase that trimethylates histone H3 'Lys-
CC 36' forming H3K36me3. Involved in transcription elongation as well as
CC in transcription repression. {ECO:0000250|UniProtKB:P46995}.
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:0000250|UniProtKB:P46995, ECO:0000255|PROSITE-
CC ProRule:PRU00901};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- DOMAIN: The AWS and SET domains are necessary for transcription
CC repression. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00901}.
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DR EMBL; GG704912; EAS30731.3; -; Genomic_DNA.
DR RefSeq; XP_001242314.2; XM_001242313.2.
DR AlphaFoldDB; Q1DU03; -.
DR SMR; Q1DU03; -.
DR STRING; 246410.Q1DU03; -.
DR PRIDE; Q1DU03; -.
DR EnsemblFungi; EAS30731; EAS30731; CIMG_06210.
DR GeneID; 4562087; -.
DR KEGG; cim:CIMG_06210; -.
DR VEuPathDB; FungiDB:CIMG_06210; -.
DR InParanoid; Q1DU03; -.
DR OMA; CQEKWIA; -.
DR OrthoDB; 453286at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IEA:InterPro.
DR GO; GO:0010452; P:histone H3-K36 methylation; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd19172; SET_SETD2; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.1740.100; -; 1.
DR Gene3D; 2.170.270.10; -; 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 Pfam; PF17907; AWS; 1.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF08236; SRI; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR SUPFAM; SSF82199; SSF82199; 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 3: Inferred from homology;
KW Chromosome; Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..1011
FT /note="Histone-lysine N-methyltransferase, H3 lysine-36
FT specific"
FT /id="PRO_0000269785"
FT DOMAIN 146..201
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 203..320
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 327..343
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT DOMAIN 604..635
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..840
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..872
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..950
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 113904 MW; BE481233774FD88D CRC64;
MAGHDDEEAR IETVKDAVTD MKLERQSSTE SVAPNGILDT ITPKDEPNGH LSSKPSTPSL
KPPKSRSRSS NSLAKDEVPE EKVGGDITIK QEPGQPPKLA RSASQKLPPR AAPLFTDLPD
KTTEATSTFQ LMEVCTYANK YLGYTEHAMD CDCAEEWDAA TCRNTACGED SDCINRATKM
ECFGDCGCGD SCQNQRFQRR EYAKVSVIKT EKKGYGLRAD CDLRPNEFIF EYIGEVINEP
QFRRRMIQYD EEGIKHFYFM SLNKGEFVDA TKKGNLGRFC NHSCNPNCYV DKWVVGEKLR
MGIFAERYIK AGEELVFNYN VDRYGADPQP CYCGEPNCTG FIGGKTQTER ATKLSHATIE
ALGIDDPDGW DTAVARRPRK KKAGEDDEEY VDSLQPKSLD ENGVTKVMAA LMQCKEKWIA
VKLLGRIQRC EDERVRHRVV RMHGYQILNS QLNTWKDDFN VVLQILDILD KFPRLTRNKI
IDSKIEGTVS PLQECDDERV AEKAKALLEI WSALEVGYRI PRMKRDPAAV NNTPTANHYE
RRETAKDDRK PNSSKSRSRS RSRSRSVDVT RNAPRGPAAL TRGGGKGHMH SYRPGQRPFR
RPFNPLPKGW FAAESNGRTY YYSATGETTW SRPTAPAVQP PPPPKRESKE KTLQDIIDGI
MNAKENTPKA KDKSATPATP ADAKIPEKKE HKEKWRSYSE EKQKKLYENT LFPHVKYIVD
KFKHKLPKDD LKRYAKEVAK KLVNSDFKNN RVEDPTKISD KQVKQVKKYC KEYFDKAVAK
HRAYEEKKAE RKSKGSVKAT TSATIDKAET TSTKAPPQFD GAAETGDEDS DVQLSDAEYE
DGQEESSHHS GLKRKRTDDE DFENDHENGG VSPTKRQRSA SLPIIPPPPP PMSPSNLVLD
DGSREALKRQ RTEGAEDDEY GDSTISSGKR QRSETPPPPP PPPPPADIPP ENIESENEND
KDQEELQDYD VQEANWGKED NIAIQSPSHS PFPAQSISNH SNTARETDSH S
