KMT_SULIR
ID KMT_SULIR Reviewed; 161 AA.
AC F0NBH8;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Protein-lysine N-methyltransferase {ECO:0000305|PubMed:23086207};
DE EC=2.1.1.- {ECO:0000269|PubMed:23086207};
DE AltName: Full=Archaeal protein lysine methyltransferase {ECO:0000303|PubMed:23086207};
DE Short=aKMT {ECO:0000303|PubMed:23086207};
GN OrderedLocusNames=SiRe_1449 {ECO:0000312|EMBL:ADX85515.1};
OS Sulfolobus islandicus (strain REY15A).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=930945;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=REY15A;
RX PubMed=21278296; DOI=10.1128/jb.01487-10;
RA Guo L., Brugger K., Liu C., Shah S.A., Zheng H., Zhu Y., Wang S.,
RA Lillestol R.K., Chen L., Frank J., Prangishvili D., Paulin L., She Q.,
RA Huang L., Garrett R.A.;
RT "Genome analyses of icelandic strains of Sulfolobus islandicus, model
RT organisms for genetic and virus-host interaction studies.";
RL J. Bacteriol. 193:1672-1680(2011).
RN [2]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, INDUCTION, AND MUTAGENESIS OF TYR-9; PRO-11; THR-12;
RP ASP-34 AND GLY-36.
RC STRAIN=REY15A;
RX PubMed=23086207; DOI=10.1128/jb.01535-12;
RA Chu Y., Zhang Z., Wang Q., Luo Y., Huang L.;
RT "Identification and characterization of a highly conserved crenarchaeal
RT protein lysine methyltransferase with broad substrate specificity.";
RL J. Bacteriol. 194:6917-6926(2012).
CC -!- FUNCTION: Catalyzes the methylation of lysine residues in target
CC proteins, using S-adenosyl-L-methionine (SAM) as the methyl donor.
CC Exhibits broad substrate specificity, being able to methylate the
CC crenarchaeal chromatin protein Cren7 primarily at 'Lys-11', 'Lys-16'
CC and 'Lys-31', as well as a number of recombinant Sulfolobus proteins in
CC vitro. Methylates lysine residues in a rather sequence-independent
CC manner. {ECO:0000269|PubMed:23086207}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000269|PubMed:23086207};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is about 60 degrees Celsius. Is active over a
CC wide temperature range, from 25 to 90 degrees Celsius. Has half-lives
CC of about 30 and 10 minutes at 80 and 90 degrees Celsius,
CC respectively. {ECO:0000269|PubMed:23086207};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23086207}.
CC -!- INDUCTION: Seems to be expressed at similar protein levels when grown
CC at 75 or 85 degrees Celsius, or in the exponential or the stationary
CC phase. {ECO:0000269|PubMed:23086207}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
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DR EMBL; CP002425; ADX85515.1; -; Genomic_DNA.
DR RefSeq; WP_012711567.1; NC_017276.1.
DR PDB; 5JWJ; NMR; -; A=1-161.
DR PDBsum; 5JWJ; -.
DR AlphaFoldDB; F0NBH8; -.
DR BMRB; F0NBH8; -.
DR SMR; F0NBH8; -.
DR STRING; 930945.SiRe_1449; -.
DR EnsemblBacteria; ADX85515; ADX85515; SiRe_1449.
DR GeneID; 7814681; -.
DR GeneID; 7940925; -.
DR GeneID; 8761611; -.
DR KEGG; sir:SiRe_1449; -.
DR eggNOG; arCOG01631; Archaea.
DR HOGENOM; CLU_068443_2_1_2; -.
DR OMA; HEFRIPG; -.
DR BRENDA; 2.1.1.B112; 8240.
DR Proteomes; UP000002664; Chromosome.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:CACAO.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026170; FAM173A/B.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13610; PTHR13610; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..161
FT /note="Protein-lysine N-methyltransferase"
FT /id="PRO_0000435795"
FT MOTIF 34..40
FT /note="DxGxGxG SAM-binding motif"
FT /evidence="ECO:0000305|PubMed:23086207"
FT MUTAGEN 1..12
FT /note="Missing: Complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:23086207"
FT MUTAGEN 1..6
FT /note="Missing: 70% of wild-type catalytic activity."
FT /evidence="ECO:0000269|PubMed:23086207"
FT MUTAGEN 9
FT /note="Y->A: 11% of wild-type catalytic activity."
FT /evidence="ECO:0000269|PubMed:23086207"
FT MUTAGEN 11
FT /note="P->A: 23% of wild-type catalytic activity."
FT /evidence="ECO:0000269|PubMed:23086207"
FT MUTAGEN 12
FT /note="T->A: 4% of wild-type catalytic activity."
FT /evidence="ECO:0000269|PubMed:23086207"
FT MUTAGEN 34
FT /note="D->K: Almost complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:23086207"
FT MUTAGEN 36
FT /note="G->R: Almost complete loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:23086207"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:5JWJ"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:5JWJ"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:5JWJ"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5JWJ"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:5JWJ"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:5JWJ"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:5JWJ"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:5JWJ"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:5JWJ"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:5JWJ"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:5JWJ"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:5JWJ"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:5JWJ"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:5JWJ"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:5JWJ"
SQ SEQUENCE 161 AA; 18154 MW; 28E9D176B4002FD3 CRC64;
MSYVPHVPYV PTPEKVVRRM LEIAKVSQDD IVYDLGCGDG RIIITAAKDF NVKKAVGVEI
NDERIREALA NIEKNGVTGR ASIVKGNFFE VDISEATVVT MFLLTNVNEM LKPKLEKELK
PGTRVVSHEF EIRGWNPKEV IKVEDGNMNH TVYLYVIGEH K
