ID A0A0C3C955_HEBCY Unreviewed; 514 AA.
AC A0A0C3C955;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Ribosomal lysine N-methyltransferase 4 {ECO:0000256|PIRNR:PIRNR011771};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR011771};
GN ORFNames=M413DRAFT_442044 {ECO:0000313|EMBL:KIM45375.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM45375.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM45375.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN831772; KIM45375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3C955; -.
DR STRING; 686832.A0A0C3C955; -.
DR HOGENOM; CLU_017135_0_0_1; -.
DR OrthoDB; 51002at2759; -.
DR Proteomes; UP000053424; 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; 2.
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 Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF011771; RMS1_SET; 2.
DR SUPFAM; SSF81822; RuBisCo LSMT C-terminal, substrate-binding domain; 1.
DR SUPFAM; SSF82199; SET domain; 1.
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:UP000053424};
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 20..299
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 187..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 57751 MW; 8749D1118B3741F5 CRC64;
MEIQPFFSWF QSHNGYVDTS TMDVIQFPPS EGGRGAIALK DIPEGHVLFS VPRTLLLSTQ
TSLLPSHFGI DAWKNFGLHK GWSGLILCMM WEAAQGSESK WKPYFDILPT KLDTPMFWSD
ADLAELAGTS VVEKLGKEEA ENDYREKIVP AVSTRPDLFP KEDLTTRYSI NTFHLMGNLI
LSRSFTLDDQ DEDEDEEEEE KEHATGDEHQ DIGNTSLGSA MDVDAPISAT NEHSEEEANE
DGDDDEETST LEVAMVPLAD ILNARYQCEN VKLFYEPDCL KMISTRPIKT GEQIWNTYGD
PPNSVLLRQY GHVDYIPLLE GGLGNPGDVV ELRADLLVQS TGAEGSIEDN PDMKERIEFW
LEEGGDDVFV LEAPSTSTSI ELPPALLSFT QLIQSEAEWE RAKSKGKLPK PKANIDTLKI
IQEALARRSK AYPTTLEEDT QLESTSLNSL SLNRRHALVV RIGEKKILER YREKVSEMIK
IMEAPQVKKP ARGGGKRKAD RDSGEIRKKR KEMR
//
