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Database: UniProt
Entry: A0A176WN16_MARPO
LinkDB: A0A176WN16_MARPO
Original site: A0A176WN16_MARPO 
ID   A0A176WN16_MARPO        Unreviewed;       336 AA.
AC   A0A176WN16;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=RNA methyltransferase {ECO:0000256|RuleBase:RU367087};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU367087};
GN   ORFNames=AXG93_4689s1220 {ECO:0000313|EMBL:OAE33636.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE33636.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE33636.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE33636.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000256|ARBA:ARBA00008361, ECO:0000256|RuleBase:RU367087}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAE33636.1}.
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DR   EMBL; LVLJ01000592; OAE33636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176WN16; -.
DR   OrthoDB; 1130801at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:GOC.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR039772; Bin3-like.
DR   InterPro; IPR010675; Bin3_C.
DR   InterPro; IPR024160; BIN3_SAM-bd_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12315:SF0; 7SK SNRNA METHYLPHOSPHATE CAPPING ENZYME; 1.
DR   PANTHER; PTHR12315; BICOID-INTERACTING PROTEIN RELATED; 1.
DR   Pfam; PF06859; Bin3; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51515; BIN3_SAM; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU367087};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU00848};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367087}.
FT   DOMAIN          69..336
FT                   /note="Bin3-type SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS51515"
SQ   SEQUENCE   336 AA;  38505 MW;  CCC3FE40EDEAE45D CRC64;
     MNDSSMGREV PVEAEDEEKQ LVHSTGVGFC DGDMSAKRKR KKPAKKEVQR FGNYHHYYGY
     RLGKSLDVDP RLNVFEPEWF EGMDCLDIGC NEGIVTISIA QKYNCRSILG LDIDEVLIRK
     AQSNLIEEAA LQGFTTGEYM EPCEAKENCS SDSENTLDNG WWKETIAWRE LTGSQQGSDR
     VEDSRCATER AERSTPLNSN NLLRRVTFRK ENVIKDFPHG DYMKDGTFDT VLCLSMTKWV
     HLNWGDDGLV RLFAKIYHIL RPGGILILEP QPWNSYRRKA KVCEVTRQNF NEIKLRPNHF
     TEILLDKIGF KSYKEVSTAV PGSTAGFDRS LYVYVK
//
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