ID A0A1D6P7L0_MAIZE Unreviewed; 624 AA.
AC A0A1D6P7L0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Methyltransferase {ECO:0000256|RuleBase:RU366043};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU366043};
GN ORFNames=ZEAMMB73_Zm00001d047183 {ECO:0000313|EMBL:AQL05819.1};
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:AQL05819.1};
RN [1] {ECO:0000313|EMBL:AQL05819.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQL05819.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU366043}; Single-
CC pass type II membrane protein {ECO:0000256|RuleBase:RU366043}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000256|ARBA:ARBA00008361, ECO:0000256|RuleBase:RU366043}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU366043}.
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DR EMBL; CM000785; AQL05819.1; -; Genomic_DNA.
DR EMBL; CM000785; AQL05830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6P7L0; -.
DR IntAct; A0A1D6P7L0; 1.
DR InParanoid; A0A1D6P7L0; -.
DR ExpressionAtlas; A0A1D6P7L0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR InterPro; IPR004159; Put_SAM_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10108:SF1051; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10108; SAM-DEPENDENT METHYLTRANSFERASE; 1.
DR Pfam; PF03141; Methyltransf_29; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|RuleBase:RU366043};
KW Membrane {ECO:0000256|RuleBase:RU366043};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU366043}; Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|RuleBase:RU366043};
KW Transferase {ECO:0000256|RuleBase:RU366043, ECO:0000313|EMBL:AQL05819.1};
KW Transmembrane {ECO:0000256|RuleBase:RU366043};
KW Transmembrane helix {ECO:0000256|RuleBase:RU366043}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..624
FT /note="Methyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010807650"
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366043"
FT TRANSMEM 95..114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366043"
SQ SEQUENCE 624 AA; 70914 MW; 6515082B041117E7 CRC64;
MLLLLLPPLS WRHAACAACC CALALAAWLM QYNHQSQHCP VCRYSTTTPR PRRVPKHNKG
ARDGTTCLRL LIEGSETLTG CGMARNLTEN RTRNTLIVIV VFGLCSFFYL LGAWQKSGSG
GGDRIQNWVN EQTKCAQLPN LSFETHHSAS NLPNDTGSSK IEPFKPCDEQ YTDYTPCEEQ
KRAMTFPRDN MIYRERHCPP DKEKLYCLIP APKGYVAPFR WPKGRDFVPY ANVPHKSLTV
EKAIQNWVHY EGNVFRFPGG GTQFPQGADK YIEQLASVIP IAEGKVRTAL DTGCGVHGMY
MMEVDRVLRP GGFWVLSGPP IGWKIHYKGW QRSKEDLRNE QRKIEHFAQL LCWKKVSEKD
GIAIWTKRLN DKSCSMKQDN PNGGKCDLTS DSDVWYKKME VCMTPLPEVN SVDEVAGGQL
EPFPKRLYAV PPRITDGSVP GFSVESYEED NNLWRKHVKA YKKINNLLDT GRYRNIMDMN
AGLGSFAAAL ESPKVWVMNV IPTIANTSTL GVIYERGLIG MYHDWCEGFS TYPRTYDLIH
SNDIFSLYQN KCQFEDILLE MDRILRPEGA IIIRDKVDVL VKVEKIANAM RWKTRLADHE
GGPHVPEKIL FAVKQYWTAE KTSS
//
