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Database: UniProt
Entry: A0A0D1YJ47_ANEMI
LinkDB: A0A0D1YJ47_ANEMI
Original site: A0A0D1YJ47_ANEMI 
ID   A0A0D1YJ47_ANEMI        Unreviewed;       419 AA.
AC   A0A0D1YJ47;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Small RNA 2'-O-methyltransferase {ECO:0000256|ARBA:ARBA00021330};
DE            EC=2.1.1.386 {ECO:0000256|ARBA:ARBA00035025};
GN   ORFNames=AF333_14500 {ECO:0000313|EMBL:KON96505.1}, SAMN04487909_10221
GN   {ECO:0000313|EMBL:SDI18053.1};
OS   Aneurinibacillus migulanus (Bacillus migulanus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=47500 {ECO:0000313|EMBL:KON96505.1, ECO:0000313|Proteomes:UP000037269};
RN   [1] {ECO:0000313|EMBL:KON96505.1, ECO:0000313|Proteomes:UP000037269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2895 {ECO:0000313|EMBL:KON96505.1,
RC   ECO:0000313|Proteomes:UP000037269};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-14205 dsm 2895.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SDI18053.1, ECO:0000313|Proteomes:UP000182836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2895 {ECO:0000313|EMBL:SDI18053.1,
RC   ECO:0000313|Proteomes:UP000182836};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; LGUG01000004; KON96505.1; -; Genomic_DNA.
DR   EMBL; FNED01000002; SDI18053.1; -; Genomic_DNA.
DR   RefSeq; WP_043064187.1; NZ_LGUG01000004.1.
DR   AlphaFoldDB; A0A0D1YJ47; -.
DR   STRING; 47500.AF333_14500; -.
DR   PATRIC; fig|47500.8.peg.1702; -.
DR   OrthoDB; 626362at2; -.
DR   Proteomes; UP000037269; Unassembled WGS sequence.
DR   Proteomes; UP000182836; Unassembled WGS sequence.
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; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR21404; HEN1; 1.
DR   PANTHER; PTHR21404:SF3; SMALL RNA 2'-O-METHYLTRANSFERASE; 1.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KON96505.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037269};
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:KON96505.1}.
FT   DOMAIN          249..369
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13847"
SQ   SEQUENCE   419 AA;  49481 MW;  19F78D1BC49DB7E9 CRC64;
     MAIIQIKSSN PDFSFIIKKN PASGMQLRSI RKGIAYGWYH GTDTYNIYFK DADTDISYKQ
     HRDETFEYLN VSRYNTPLLP LNAIAEFLSA TFKNKNEKDK DGYENSFFVN MIHIKYPRYI
     DFFNKHFTDF HIEIEQHTHK SYKMTIKSNR SIYKLVNFAN VLFLFLAMLG KEYLGVSDSL
     VEKYLKSMNI IDAPYYIRYL FARNVLINKE IFYKFKKELE QTDKYAINFV FGNTAIQRKQ
     FIEKGISFDK SILDIGCGEG FYALPFSGKI EDNFYYAIDI NEELIREVDI KAKKRNIENL
     ITFPSLHTYL ESYSGEVVDV LLTEVIEHMD VPEAELLVKS VYENVKFDKF IITTPNYDFN
     QYYALNEFRH SDHKWEMNKN EFEKWIHDMF KETNYTLQFL NIGDSVDGVY TTQGVLITT
//
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