GenomeNet

Database: UniProt
Entry: H2VCX5_TAKRU
LinkDB: H2VCX5_TAKRU
Original site: H2VCX5_TAKRU 
ID   H2VCX5_TAKRU            Unreviewed;       247 AA.
AC   H2VCX5;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=RNA methyltransferase {ECO:0000256|RuleBase:RU367087};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU367087};
GN   Name=BCDIN3D {ECO:0000313|Ensembl:ENSTRUP00000047068.2};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000047068.2, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000047068.2, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000047068.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-phospho)-ribonucleoside-RNA + 2 S-adenosyl-L-
CC         methionine = a 5'-end (5'-bismethylphospho)-ribonucleoside-RNA + 2 S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:58640, Rhea:RHEA-COMP:15179,
CC         Rhea:RHEA-COMP:15182, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138282, ChEBI:CHEBI:142777;
CC         Evidence={ECO:0000256|ARBA:ARBA00036615};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-phospho)-ribonucleoside-RNA + S-adenosyl-L-
CC         methionine = a 5'-end (5'-methylphospho)-ribonucleoside-RNA + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:58656, Rhea:RHEA-COMP:15179,
CC         Rhea:RHEA-COMP:15181, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:138282, ChEBI:CHEBI:142776;
CC         Evidence={ECO:0000256|ARBA:ARBA00036772};
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000256|ARBA:ARBA00008361, ECO:0000256|RuleBase:RU367087}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_011611992.1; XM_011613690.1.
DR   AlphaFoldDB; H2VCX5; -.
DR   STRING; 31033.ENSTRUP00000047068; -.
DR   Ensembl; ENSTRUT00000047227.3; ENSTRUP00000047068.2; ENSTRUG00000018395.3.
DR   GeneID; 105417806; -.
DR   KEGG; tru:105417806; -.
DR   CTD; 144233; -.
DR   eggNOG; KOG2899; Eukaryota.
DR   GeneTree; ENSGT00940000153993; -.
DR   HOGENOM; CLU_082749_0_0_1; -.
DR   InParanoid; H2VCX5; -.
DR   OMA; RKICFYR; -.
DR   OrthoDB; 1130801at2759; -.
DR   Proteomes; UP000005226; Chromosome 19.
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: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; 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; BICOID-INTERACTING PROTEIN RELATED; 1.
DR   PANTHER; PTHR12315:SF1; RNA 5'-MONOPHOSPHATE METHYLTRANSFERASE; 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:UP000005226};
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          35..247
FT                   /note="Bin3-type SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS51515"
SQ   SEQUENCE   247 AA;  28221 MW;  0B6DE9DF72DA57D2 CRC64;
     MATCSPNTDR TDEINDPGAA PFGNFINYYT FNPPENRLNL IPATLLRDLD YNGDTTLILD
     VGCNSGELST AFYKHLVPDC EEQSDDSKVY LLGFDLDEIL IQRAQQTNSL PSSISFITMD
     IIKDTEQLQH YLDQHGCSSF HLCLCLAVTM WIHLNHGDSG LLQLLSRLAT FSQHLLLEAQ
     PWKCYRSAAR RLRKLGRSDF DHFKTLNIRG DIAEHAREHL ENHCGMELIQ SFGSTSWDRK
     LLLFKRR
//
DBGET integrated database retrieval system