ID A5AXD0_VITVI Unreviewed; 507 AA.
AC A5AXD0;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=SET domain-containing protein {ECO:0000259|PROSITE:PS50280};
GN ORFNames=VITISV_015206 {ECO:0000313|EMBL:CAN82664.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CAN82664.1};
RN [1] {ECO:0000313|EMBL:CAN82664.1}
RP NUCLEOTIDE SEQUENCE.
RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT vinifera L.): coping with a highly heterozygous genome.";
RL PLoS ONE 2:e1326-e1326(2007).
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}.
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DR EMBL; AM439109; CAN82664.1; -; Genomic_DNA.
DR EnsemblPlants; Vitvi01g01058_t001; Vitvi01g01058_P001; Vitvi01g01058.
DR Gramene; Vitvi01g01058_t001; Vitvi01g01058_P001; Vitvi01g01058.
DR ExpressionAtlas; A5AXD0; baseline and differential.
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 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|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00916};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR009328-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 61..284
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT BINDING 77..79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 239..240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
SQ SEQUENCE 507 AA; 57138 MW; B38037AD300DA037 CRC64;
MATLFTLVSS SSSVFFFPIK TLKNPPIIHS RRPPFSLTCL RSLETNPPPP VQTFWKWLFD
QGVVSGKTPV KPGIVPEGLG LVAQRDIARN EAVLEVPKRF WINPDAVAAS EIGSVCGGLK
PWVSVALFLI REKLRDESPW RSYLDILPEY TNSTIYWSEE ELVEIQGTQL SNTTLGVKEY
VQSEFLKVEE EVILPHSQLF PFPVTLDDFL WAFGILRSRA FSRLRGQNLV LIPLADLINH
SPSITTEEYA WEIKGAGLFS RDQLFSLRTP VSVKAGEQVL IQYDLDKSNA ELALDYGFIE
SRPNRNSYTL TLEISESDPF FGDKLDIAES NGLSEIAYFD IVLGQSLPAA MLPYLRLVAL
GGPDAFLLES IFRNTIWGHL ELPVSRANEE LICQVIQDAC KSALSGYLTT IEEDEKLKEE
GNLHPRLEIA VGVRTGEKKV LQQIDGIFRE RERELDQLEY YQERRLKDLG LCGEQGVSLY
GVLKMEKEXS QRTTLNHLGL LVAIVTY
//
