ID T2MC08_HYDVU Unreviewed; 423 AA.
AC T2MC08;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Small RNA 2'-O-methyltransferase {ECO:0000256|ARBA:ARBA00021330};
DE EC=2.1.1.386 {ECO:0000256|ARBA:ARBA00035025};
GN Name=HENMT1 {ECO:0000313|EMBL:CDG69611.1};
GN Synonyms=LOC100200697 {ECO:0000313|RefSeq:XP_002166393.2};
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG69611.1};
RN [1] {ECO:0000313|EMBL:CDG69611.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole animals {ECO:0000313|EMBL:CDG69611.1};
RX PubMed=24065732; DOI=10.1093/gbe/evt142;
RA Wenger Y., Galliot B.;
RT "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT bilaterian, euteleostome, and hominidae ancestors.";
RL Genome Biol. Evol. 5:1949-1968(2013).
RN [2] {ECO:0000313|RefSeq:XP_002166393.2}
RP IDENTIFICATION.
RC STRAIN=105 {ECO:0000313|RefSeq:XP_002166393.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) +
CC S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide;
CC Xref=Rhea:RHEA:37887, Rhea:RHEA-COMP:10415, Rhea:RHEA-COMP:10416,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74896, ChEBI:CHEBI:74898; EC=2.1.1.386;
CC Evidence={ECO:0000256|ARBA:ARBA00034992};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family.
CC {ECO:0000256|ARBA:ARBA00009026}.
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 EMBL; HAAD01003379; CDG69611.1; -; mRNA.
DR RefSeq; XP_002166393.2; XM_002166357.3.
DR EnsemblMetazoa; XM_002166357.3; XP_002166393.2; LOC100200697.
DR GeneID; 100200697; -.
DR KEGG; hmg:100200697; -.
DR OrthoDB; 2735228at2759; -.
DR Proteomes; UP000694840; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR026610; Hen1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR21404; HEN1; 1.
DR PANTHER; PTHR21404:SF3; SMALL RNA 2'-O-METHYLTRANSFERASE; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CDG69611.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000694840};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDG69611.1}.
SQ SEQUENCE 423 AA; 49546 MW; 5CDA5BE3B96074E1 CRC64;
MEITRESVFN PPLFKQRYEA VAQIINQTQA KSVLDIGCSE GKFLTYMKEK CTSVEKIIGV
DIDRSLLENN TYFIQPKPFE YIVKRTVPLN ISLFCGSITQ SDVRFHHVDF ISCIEVIEHL
YDDVLSMVPY NIFGILKPKT VVITTPNAEY NQLFKGFSGL RHNDHKFEWT RNQFQQWCSR
IERTYGYNVE FDGVGAPPAD SKVGYCSQIA VFRQTDNKLP IEHNDLEYLM DLHSGVICHH
ASENDGVCHR SLDEVIVPLC QKFNCNQIEV CHCTSYKTKL NKYKSFENVE NFSLVYQVEY
PYDNLSLNLE QKILDEIGYN IFLFFSDTDD QLEEVIEKRV PVKFFHSLSS IAKFNVNCDQ
LTSIIRQKFR ISDDNQHVIF NVTLNSRQWY NYSDDDIEEE DEKRYEPSNE FIIDHIEEEE
SWD
//
