ID A0A0D7AVC2_9AGAR Unreviewed; 995 AA.
AC A0A0D7AVC2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=SET domain-containing protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CYLTODRAFT_427015 {ECO:0000313|EMBL:KIY62328.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY62328.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY62328.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY62328.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KN880796; KIY62328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7AVC2; -.
DR STRING; 1314674.A0A0D7AVC2; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000054007; 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 H3K36 methyltransferase activity; IEA:UniProt.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR013257; SRI.
DR InterPro; IPR038190; SRI_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; PF00856; SET; 1.
DR Pfam; PF08236; SRI; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054007};
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 142..197
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 199..336
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 343..359
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..949
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..972
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 995 AA; 110086 MW; 72682A271FC67F04 CRC64;
MASEHAESYT DSGPSTRGTP PPPPTPAAPT PPAAPTPPSS SMSAEDLFAG DPPDTSVPST
AGPSRTPTPT PTPTPAPKNT STAQHNTTAP VPKKPAKSKK PSRAVQLITE LPIALEEACK
TFEVLKESRY QSKKLGASQE LLEGSMCDCV FSPGKDDPED ACGERSDCIN RLTQVECDPR
ECKCRGFCRN QRFQKREYAH ITVVQTEKKG FGLRAEEDIP RDGFIMEYVG DVVNEKSFKK
RLHDYAAKGI KHFYFMMLQK GAYIDATTAG GIGRFANHSC APNCFVAKWT VPSSVGAGAS
ASSSYYSTSS SQSMVRMGIF AKRAIARGEE LTFDYNVDRY GFEAQTCWCG EPECVGFIGG
KTQTVSDDTL AALGIEVGDV DRPEVRLKMK RQRQGKLGKG LGLGLGGELG EGKLDVLSPL
EVRDVPKVLQ AIRANVGRKE VLQKLLRRVE MTEDMAVLRQ CMRLRALTLF KTLLEDALGV
VKPAAQEEEE EQAKEGEATS TPSLGSPREG GTAEPELSTP PPQTQVDPDM AVLIMQCLTT
WPLVQRNKVL DSKILDTLDA CIAKAPLLPT PPPAVDKAEG TQAEAEAEGR RCAVLAGELK
VKWEALEVAY RIPKRKMDPN QIIEDSPSAA GQEDSLDDVS VPTPDPNPNP NPKLAVEPTP
KRPRMDEKRK PARPPRPHVQ SFRLLTPPPP PPPPPRLKPS VSWTATLSSS SQSKLDKYKQ
EAERRLEEEA AQKDAERLKE VERKAKKQKE AERRERKERR RREWEEQKER RMRKLVGVEV
MEVMNKYCGG RVDRERFKRY AKELTHIIAT KEQKSPKYAT LKYDAPFEGE KAKKVKAYAK
EYIAKVLRRL KQEGKLQEGG KTHTQEGKMH TQEGGKMQEG REERRGEVMT LEETFDLEVG
HEERDREKHE EEEEGEGEEG EGDMELSDDE EDVRIPGEEM PEDGGEYEER VADADAMVEG
EGEGEGEDPM DVDPPSYEVA MGQTKSVVEL GAPGP
//
