ID A0A1U8HSX8_GOSHI Unreviewed; 488 AA.
AC A0A1U8HSX8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Fructose-bisphosphate aldolase-lysine N-methyltransferase, chloroplastic-like {ECO:0000313|RefSeq:XP_016667068.1};
GN Name=LOC107887371 {ECO:0000313|RefSeq:XP_016667068.1};
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016667068.1};
RN [1] {ECO:0000313|Proteomes:UP000189702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX PubMed=25893780; DOI=10.1038/nbt.3208;
RA Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT provides insights into genome evolution.";
RL Nat. Biotechnol. 33:524-530(2015).
RN [2] {ECO:0000313|RefSeq:XP_016667068.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_016667068.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_016667068.1; XM_016811579.1.
DR AlphaFoldDB; A0A1U8HSX8; -.
DR STRING; 3635.A0A1U8HSX8; -.
DR PaxDb; 3635-A0A1U8HSX8; -.
DR GeneID; 107887371; -.
DR KEGG; ghi:107887371; -.
DR OrthoDB; 51002at2759; -.
DR Proteomes; UP000189702; Chromosome 12.
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; IBA:GO_Central.
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}; Reference proteome {ECO:0000313|Proteomes:UP000189702};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR009328-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 65..288
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 243..244
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009328-1"
SQ SEQUENCE 488 AA; 54929 MW; 1261B65BEDE49328 CRC64;
MAPSLFTLSS PSSSFPSSST TLKPFSSFST KPTLSIHFVK KPIPVSATAD PPPQLQTFWQ
WLQDQGVVSA KSPVRPGMVP EGLGLIAKKN ISRNEVVLEI PNRFWINQDA VVASEIGTVC
SGLKPWVSVA LFLIRERFRQ DSKWGVYLDI LPELTDSTVF WSEEELAELQ GTQLLSTTLG
VKEYVQNEFL KVEEEIILPN KQLFPAPITL DDFFWAFGIL RSRAFSRLRG QNLVLIPLAD
LINHSPNITT EDYAWEIKGA GLFSRDLLFS LRSPVSVKAE EQVLIQYDLD KSNAELALDY
GFIESKSERN AYTLTLEISE SDPFFGDKLD IAETNGLSET AYFDIVLGRP LPPALIPYLR
LVALGGTDAF LLESIFRNTI WGHLDLPVSR ANEELICRVV RDACKSALSG YHTTIEEDEK
LMEDENLDSR LKIAVGIRAG EKKVLQQIDE IFKGRESELD ELEYYQERRL KDLGLVGEQG
EIIFWETN
//
