ICS2_CAMIR
ID ICS2_CAMIR Reviewed; 364 AA.
AC Q2HXI7;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Probable methyltransferase ICS2 {ECO:0000303|PubMed:16333668};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q2HXL9};
GN Name=ICS2 {ECO:0000303|PubMed:16333668};
OS Camellia irrawadiensis (Burmese tea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Theaceae; Camellia.
OX NCBI_TaxID=153142;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=16333668; DOI=10.1007/s00438-005-0070-z;
RA Yoneyama N., Morimoto H., Ye C.-X., Ashihara H., Mizuno K., Kato M.;
RT "Substrate specificity of N-methyltransferase involved in purine alkaloids
RT synthesis is dependent upon one amino acid residue of the enzyme.";
RL Mol. Genet. Genomics 275:125-135(2006).
CC -!- FUNCTION: No detectable N-methyltransferase activity.
CC {ECO:0000269|PubMed:16333668}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9FLN8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AB207816; BAE79731.1; -; mRNA.
DR AlphaFoldDB; Q2HXI7; -.
DR SMR; Q2HXI7; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.270; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR005299; MeTrfase_7.
DR InterPro; IPR042086; MeTrfase_capping.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31009; PTHR31009; 1.
DR Pfam; PF03492; Methyltransf_7; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Magnesium; Metal-binding; Methyltransferase; Transferase.
FT CHAIN 1..364
FT /note="Probable methyltransferase ICS2"
FT /id="PRO_0000451789"
FT BINDING 18
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 21..25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 60..61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0A6C0WW36"
FT BINDING 96..99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 133..135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 150..152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 151..155
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT SITE 148
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 220
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q2HXI6"
FT SITE 264
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 312
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 327
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
SQ SEQUENCE 364 AA; 40679 MW; D8A38065E76DDCC8 CRC64;
MEVKEALFMN KGEGESSYAQ SSSFTETVTS MTMPVLENAV ETLFSKDFHL LQALNAADLG
CAAGPTTFTV ISTIKRMMEK KCRELNCQTL ELQVYLNDLP GNDFNTLFKG LSSKVVGNKC
EEVPCYVVGV PGSFHGRLFP RNSLHLVHSC YSVHWLTQAP KGLTSKEGLA LNKGKIYISK
TSPPVVREAY LSQFHEDFTM FLNSRSQEVV PNGCMVLILR GRLSSDPSDM ESCFTWELLA
VAIAELVSQG LIDEDKLDTF NVPSYFPSLE EVKDIVERNG SFTIDHMEGF ELDSPQMQEN
DKWVRGEKFA TVARAFTEPI ISNQFGHEIM DKLYEKFTHI VVSDLEAKIP KITSIILVLS
KIVG
