ID A0A1D6G5X3_MAIZE Unreviewed; 465 AA.
AC A0A1D6G5X3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=S-adenosyl-L-methionine-dependent methyltransferase superfamily protein {ECO:0000313|EMBL:AQK98610.1};
GN ORFNames=ZEAMMB73_Zm00001d012029 {ECO:0000313|EMBL:AQK98610.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK98610.1};
RN [1] {ECO:0000313|EMBL:AQK98610.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK98610.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01024}.
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DR EMBL; CM000784; AQK98610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6G5X3; -.
DR SMR; A0A1D6G5X3; -.
DR IntAct; A0A1D6G5X3; 1.
DR InParanoid; A0A1D6G5X3; -.
DR OMA; CVINVGP; -.
DR ExpressionAtlas; A0A1D6G5X3; baseline and differential.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR47548; BNAA06G32370D PROTEIN; 1.
DR PANTHER; PTHR47548:SF1; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR Pfam; PF03602; Cons_hypoth95; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01024}.
FT BINDING 287
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 314
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 337
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 385
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 465 AA; 51065 MW; 8F4536B4FFE11A7D CRC64;
MPPPAGLPPW PTPSTTRLAT PTPTRPPPRT THVRPPPPPY TRVRLPPPPP ATTPLPPRLE
PAAPKPAAVA TLLPPSTASA ASSSSTCLDC VHFGKCSGCT HEVDLDKPPV LQEVANFFKG
HGVGDFTFSR GRLSQWRCRA KLAVRGTPEN PLIGLYQEGT HAVIDIPECR AHHPSINAAV
KLLRQGITEL SIQPFDEDAG AGELRYVQMA VTTYNTSIPV DKRYEQGKVQ VSLVWNSRDE
RSQNAEKLTS IIEIIFGHKW RHLKGERDMW ERYGGVDISL DPCSFGQANT LSFNSLLHKL
NKYVPRSSTV VDLYSGAGVI GLSVAASRKC RSVKCIEINK QSKMSFETSA SRLPANLGCT
ITWHNTDASV EPSHWLEGSS VVIVDPPRKG LHPSVISALQ KVALSERKAY KAKRLRMRRD
HGSYGQGRLQ FMLIIQQLKR AMKRGLKLSY TLAVDGKVLR GTAKA
//
