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Database: UniProt
Entry: S8CF59_9LAMI
LinkDB: S8CF59_9LAMI
Original site: S8CF59_9LAMI 
ID   S8CF59_9LAMI            Unreviewed;       463 AA.
AC   S8CF59;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=SET domain-containing protein {ECO:0000259|PROSITE:PS50280};
DE   Flags: Fragment;
GN   ORFNames=M569_09282 {ECO:0000313|EMBL:EPS65495.1};
OS   Genlisea aurea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX   NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS65495.1, ECO:0000313|Proteomes:UP000015453};
RN   [1] {ECO:0000313|EMBL:EPS65495.1, ECO:0000313|Proteomes:UP000015453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23855885;
RA   Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA   Logacheva M.D.;
RT   "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT   number of genes and short non-coding sequences.";
RL   BMC Genomics 14:476-476(2013).
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Plant protein-lysine LSMT methyltransferase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU00916}.
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:EPS65495.1}.
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DR   EMBL; AUSU01004192; EPS65495.1; -; Genomic_DNA.
DR   AlphaFoldDB; S8CF59; -.
DR   OrthoDB; 51002at2759; -.
DR   Proteomes; UP000015453; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:InterPro.
DR   GO; GO:0030785; F:[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd19179; SET_RBCMT; 1.
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; IPR011192; Rubisco_LSMT_MeTrfase_plant.
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   InterPro; IPR044431; SET_RBCMT.
DR   PANTHER; PTHR13271:SF113; [FRUCTOSE-BISPHOSPHATE ALDOLASE]-LYSINE N-METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1.
DR   Pfam; PF09273; Rubis-subs-bind; 1.
DR   PIRSF; PIRSF009328; RMT_SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF81822; RuBisCo LSMT C-terminal, substrate-binding domain; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51583; SAM_MT127; 1.
DR   PROSITE; PS50280; SET; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00916};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR009328-1};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00916}.
FT   DOMAIN          37..262
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   BINDING         53..55
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         196
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         216..217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         261
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EPS65495.1"
FT   NON_TER         463
FT                   /evidence="ECO:0000313|EMBL:EPS65495.1"
SQ   SEQUENCE   463 AA;  53054 MW;  21B4C74A80AF4916 CRC64;
     SPALHFNRRS LSAKSSSLSA AQVPPEIDRF WQWLRDEKVI SSRTPVEPAV VPEGLGLVAT
     RDISKNDVVL EVPRRFWIHP DAVAASDIGT VCSGLKPWIS VALFLIRERF KGEESQWRYY
     LEILPRSTNS TIYWSDEELL EIRGTQLLGT TLGVKEYVEK EFDKVEEEVI LANENLFPFR
     VTTDDFMWAF GILRSRAFSR LRNRNLVIVP FADLLNHSAA VSTEDHAHEV GGPAGLFSWD
     YLFQIRSPLS LKSGDQVFIQ YDLKKSNADM ALDYGFIESE PGRDAFTLTL EIPESDEFYD
     DKLDVAESNG MERTAYFDVK YDRRLPQGML PFLRLLALGG TDAFLLEALF RNQVWGFLQL
     PVSRPNEEHV CRVVRSACRD ALSGYHTTVE QDEKILSEMG ECGDGRLRMA VGVRRGEKRV
     LQQIDEMFRV RESELDSLEY YQERRMKDLG LLGQKGEIIF WET
//
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