ID A0A2S5BI44_9BASI Unreviewed; 498 AA.
AC A0A2S5BI44;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Ribosomal lysine N-methyltransferase 4 {ECO:0000256|PIRNR:PIRNR011771};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR011771};
GN ORFNames=BMF94_0641 {ECO:0000313|EMBL:POY76441.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY76441.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY76441.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY76441.1,
RC ECO:0000313|Proteomes:UP000237144};
RX PubMed=29375494;
RA Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL Front. Microbiol. 8:2528-2528(2018).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N-
CC methyltransferase that monomethylates 60S ribosomal protein L42.
CC {ECO:0000256|PIRNR:PIRNR011771}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR011771}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SETD6 subfamily.
CC {ECO:0000256|PIRNR:PIRNR011771}.
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:POY76441.1}.
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DR EMBL; PJQD01000005; POY76441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5BI44; -.
DR STRING; 741276.A0A2S5BI44; -.
DR OrthoDB; 51002at2759; -.
DR Proteomes; UP000237144; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1420.10; Rubisco LSMT, substrate-binding domain; 1.
DR Gene3D; 3.90.1410.10; set domain protein methyltransferase, domain 1; 1.
DR InterPro; IPR011383; N-lys_methylase_SETD6.
DR InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR13271:SF34; N-LYSINE METHYLTRANSFERASE SETD6; 1.
DR PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1.
DR Pfam; PF09273; Rubis-subs-bind; 1.
DR PIRSF; PIRSF011771; RMS1_SET; 3.
DR SUPFAM; SSF81822; RuBisCo LSMT C-terminal, substrate-binding domain; 1.
DR SUPFAM; SSF82199; SET domain; 2.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR011771};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR011771};
KW Reference proteome {ECO:0000313|Proteomes:UP000237144};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR011771};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR011771}.
FT DOMAIN 23..304
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 56..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 55597 MW; A5AAC4CE68494D3E CRC64;
MSSSSGEQTF VDWFKARGGT VHDAVGFKQF EGQGRGCVAL QDIESELLSR PSVGSTRLAR
SLNEQQRSAE STTTARSEEV SERRRGADIR PRPQADTVLF SIPRPILLTT STAALPTLLP
AEEWAELGGW TPLILSMMYE YLRTSTWQPY FALLPTEFDS LMFWSDEELA QLEGSTVLGK
IGREEANETF DETVKPFVEK HAAVFGDASD YSAELFHRMG SLVLSRSFHV DSKPDVDDED
DDEDSDDEEE EREDVADVAM VPFADILNAK SGANNARLFY EPTTLNMMST THIPAGAQIY
NTYADPPNPD LLRRYGHVDE VNEADLVEIG LETVVDLVGE ARGMGEEERE ARAEWLLEMG
IDDTFSIETN HKLPDELVSA IRAFSLSDED FAKAQKKESP PKPKLDAESA AWARKIVEQR
LGEYKTTVEE DEALLQDGSI PLRRRMAVIV RLGEKRLLQG AKSKLDAEWP EGEAKPATQD
KKRSRDAKDG GRKKKAKQ
//
