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Database: UniProt
Entry: A0A2G9GDV1_9LAMI
LinkDB: A0A2G9GDV1_9LAMI
Original site: A0A2G9GDV1_9LAMI 
ID   A0A2G9GDV1_9LAMI        Unreviewed;       498 AA.
AC   A0A2G9GDV1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=N-methyltransferase {ECO:0000313|EMBL:PIN03459.1};
DE            EC=2.1.1.127 {ECO:0000313|EMBL:PIN03459.1};
GN   ORFNames=CDL12_24002 {ECO:0000313|EMBL:PIN03459.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN03459.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
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:PIN03459.1}.
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DR   EMBL; NKXS01005513; PIN03459.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G9GDV1; -.
DR   STRING; 429701.A0A2G9GDV1; -.
DR   OrthoDB; 169378at2759; -.
DR   Proteomes; UP000231279; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:InterPro.
DR   GO; GO:0030785; F:[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
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:SF123; RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE_OXYGENASE SMALL SUBUNIT N-METHYLTRANSFERASE I-RELATED; 1.
DR   PANTHER; PTHR13271; UNCHARACTERIZED PUTATIVE METHYLTRANSFERASE; 1.
DR   Pfam; PF09273; Rubis-subs-bind; 1.
DR   Pfam; PF00856; SET; 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; PS50280; SET; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:PIN03459.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRSR:PIRSR009328-1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PIN03459.1}.
FT   DOMAIN          83..299
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   BINDING         241
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         262..263
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT   BINDING         310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
SQ   SEQUENCE   498 AA;  56701 MW;  81C039FCA36C69D4 CRC64;
     MAEDSRILQA TLIHTFGQNP SQYTLRIHSP CYNPPSISKR SGSLRCSVST ASSGGVPWGC
     DIDSLENAAA LQKWLSECGL PPQKMAIQRV EIGERGLVAL KNIRKGEKLL FVPPSLFITA
     DSEWTCLEAG QVLKRAHVPD WPLLATYLIS EASLINSSRW SNYISALPRQ PYSLLYWTRS
     ELDRYLEASQ IRERAIERIN DVIGTYIDLK ERIFSKYPDL FPEEVFNMES FLWSFGILFS
     RLVRLPSMDG RVALVPWADM LNHSCEVETF LDYDKSSQGV VFTTDRAYQP GEQVFISYGK
     KSNGELLLSY GFVPREGTNP RDSVELLLSL KKSDKCYKEK SEALKKYGLS ASQCFPLQIT
     GWPVELMAYA YLAVSPPSMR NRFDEMAAEA SNKTKPKKDT RYPEIEEDAL QFILDACEAS
     ISKYSKFLQA SGSMDLDVTN PKLLNRKVFL KQLAVDLCTS EQRILFRAQY ILRRRLRDIR
     SGELRALKIF NGFRKLFN
//
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