ID A0A0B2QS52_GLYSO Unreviewed; 278 AA.
AC A0A0B2QS52;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Alpha N-terminal protein methyltransferase 1 {ECO:0000256|ARBA:ARBA00039449};
DE EC=2.1.1.244 {ECO:0000256|ARBA:ARBA00039112};
DE AltName: Full=X-Pro-Lys N-terminal protein methyltransferase 1 {ECO:0000256|ARBA:ARBA00043129};
GN ORFNames=glysoja_037433 {ECO:0000313|EMBL:KHN22939.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN22939.1};
RN [1] {ECO:0000313|EMBL:KHN22939.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Root {ECO:0000313|EMBL:KHN22939.1};
RA Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT "Identification of a novel salt tolerance gene in wild soybean by whole-
RT genome sequencing.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-
CC L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54712, Rhea:RHEA-COMP:13785, Rhea:RHEA-COMP:13971,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:138057, ChEBI:CHEBI:138315; EC=2.1.1.244;
CC Evidence={ECO:0000256|ARBA:ARBA00035913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal L-prolyl-L-prolyl-L-lysyl-[protein] + 2 S-adenosyl-
CC L-methionine = 2 H(+) + N-terminal N,N-dimethyl-L-prolyl-L-prolyl-L-
CC lysyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54736,
CC Rhea:RHEA-COMP:13787, Rhea:RHEA-COMP:13974, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:138059,
CC ChEBI:CHEBI:138318; EC=2.1.1.244;
CC Evidence={ECO:0000256|ARBA:ARBA00036157};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal L-seryl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-
CC L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-seryl-L-prolyl-
CC L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54724, Rhea:RHEA-COMP:13789, Rhea:RHEA-COMP:13973,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:138061, ChEBI:CHEBI:138317; EC=2.1.1.244;
CC Evidence={ECO:0000256|ARBA:ARBA00036171};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. NTM1 family.
CC {ECO:0000256|ARBA:ARBA00009059}.
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DR EMBL; KN656751; KHN22939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2QS52; -.
DR Proteomes; UP000053555; Unassembled WGS sequence.
DR GO; GO:0047874; F:dolichyldiphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR008576; MeTrfase_NTM1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12753; AD-003 - RELATED; 1.
DR PANTHER; PTHR12753:SF0; ALPHA N-TERMINAL PROTEIN METHYLTRANSFERASE 1; 1.
DR Pfam; PF05891; Methyltransf_PK; 1.
DR PIRSF; PIRSF016958; DUF858_MeTrfase_lik; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KHN22939.1};
KW Methyltransferase {ECO:0000313|EMBL:KHN22939.1};
KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR016958-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KHN22939.1}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
FT BINDING 151..152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
FT BINDING 167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR016958-1"
SQ SEQUENCE 278 AA; 31342 MW; 398103259B271587 CRC64;
MDAAGLDSDG REFKTPDDMW REQAGDPSKK TQWYRDGVSY WEGVKANMDG VLGGFANVNE
PDISCSEDFL NILLSERFPP AADARRQPLV ALDCGSGIGR VTKNLLIRYF NEVDLLEPVS
HFLETARETL ASGCQTNSDM HKAVNFYCVP LQDFTPDTAR YDVIWIQWCI GHLTDEDFVS
FFKSAKVGLK AGGFFVLKEN IARSGFVLDN EDRSVTRSDL YFKELFSRCG LHVYKSKDQK
GFPEELFAVK MYALTTDPPK KAPRAKSKTS TNRPKTIM
//
