ID A0A1V6U0T7_9EURO Unreviewed; 910 AA.
AC A0A1V6U0T7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=SET domain-containing protein 5 {ECO:0000256|ARBA:ARBA00042380};
GN ORFNames=PENSTE_c001G04877 {ECO:0000313|EMBL:OQE31820.1};
OS Penicillium steckii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=303698 {ECO:0000313|EMBL:OQE31820.1, ECO:0000313|Proteomes:UP000191285};
RN [1] {ECO:0000313|Proteomes:UP000191285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24891 {ECO:0000313|Proteomes:UP000191285};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQE31820.1}.
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DR EMBL; MLKD01000001; OQE31820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6U0T7; -.
DR OrthoDB; 2259237at2759; -.
DR Proteomes; UP000191285; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR46402:SF2; HISTONE-LYSINE N-TRIMETHYLTRANSFERASE SMYD5; 1.
DR PANTHER; PTHR46402; SET AND MYND DOMAIN-CONTAINING PROTEIN 5; 1.
DR Pfam; PF00856; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000191285};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 477..835
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 910 AA; 105082 MW; F0C94999AFF196B7 CRC64;
MSDQPSTYTR STNEPTRFLT GRRGIAQQKR ANLGPGHEPD WTWVRSDGLR RFGDAFKARP
PWTAIRSAEW PPKPGHTGKT IDFGSFVTKT DAKLAYDIWK LADDTVGDAW KNRDRQLPTS
KAKEPGLANN VYEHLMIYSV LPLDRREAPQ VFSQQGLKKT WNVAAMIDSL KDKIIEESPI
RGVTNWTSQA LKNELKKRDL SAAGNSKKLQ QRLIDDEVQN HCGIMPTSDL SQWGIKRKSK
FILQPATNTE MTPLDMYTFA IHLSPYNPTY WLSRAYCHYL QGYFDLALGD AYRAQIICNT
VEQLNERNSK DGFFTHIQHA IHQHILVYPK DEEGYWSELI TLMRKPHGIQ SMITSIHFAV
LNIICLCLAA LNCWDDFDAY TKQLSMRAGS IFPEKFVADL RKKVSKKASR AWRRKKSKQN
LFWFEKHQGA VSAERSYPYE NNPLEQIPEK RPLLGRLTEE IFQHQKVRED HPDVPTDTCQ
VKMAPDRLRY GVFAKRRIRK GELIHFEEPT IRGHLPPRRL TKDRTHTKFV DDHRCEHCLD
LVNDRERRPS IDDIRSAHPD EIDADEVPYC TCLRHWLRNP HDKKGLMFCP SDSKETSCLQ
IAYDLYHYDG CGRNWTWLYD TMRPNVWTWS GMQHISHSNE VHGTHLSLLL RSVAETTLLR
REDYDEPGLA PYEIDEILIL NGNSKSWRSS WFPFTMSANI IVPFDIFSFL GINIFRDFSF
DTWALQIIMR KLLVNAVPWD MKRRGNIRTV LTTDKEKILD SPAQQVRRLM NGYSLGEWDP
SFLNLYLFSG LSLFNHTCAG KENAEWAYDS QVLNRVIVWA KKNIEVGEEI RIRYQNDTVD
SRGDAARLFG GPCLCPHKSK HNTVDESESD EESTSKETSV SLLMSNVALS DDSSESEDGW
LARAEGKTES
//