ID A0A495X8Y5_9PSEU Unreviewed; 457 AA.
AC A0A495X8Y5;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Small RNA 2'-O-methyltransferase {ECO:0000256|ARBA:ARBA00021330};
DE EC=2.1.1.386 {ECO:0000256|ARBA:ARBA00035025};
GN ORFNames=DFJ66_2266 {ECO:0000313|EMBL:RKT69073.1};
OS Saccharothrix variisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT69073.1, ECO:0000313|Proteomes:UP000272729};
RN [1] {ECO:0000313|EMBL:RKT69073.1, ECO:0000313|Proteomes:UP000272729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT69073.1,
RC ECO:0000313|Proteomes:UP000272729};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) 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}.
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:RKT69073.1}.
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DR EMBL; RBXR01000001; RKT69073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495X8Y5; -.
DR OrthoDB; 626362at2; -.
DR Proteomes; UP000272729; 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; 3.30.1610.20; Hen1, N-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR024026; 3'-RNA_MeTfrase_Hen1_bac.
DR InterPro; IPR026610; Hen1.
DR InterPro; IPR024740; Hen1_N.
DR InterPro; IPR038546; Hen1_N_sf.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR04074; bacter_Hen1; 1.
DR PANTHER; PTHR21404; HEN1; 1.
DR PANTHER; PTHR21404:SF3; SMALL RNA 2'-O-METHYLTRANSFERASE; 1.
DR Pfam; PF12623; Hen1_L; 1.
DR Pfam; PF08242; Methyltransf_12; 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:RKT69073.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000272729};
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:RKT69073.1}.
FT DOMAIN 1..229
FT /note="Hen1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12623"
FT DOMAIN 278..369
FT /note="Methyltransferase type 12"
FT /evidence="ECO:0000259|Pfam:PF08242"
SQ SEQUENCE 457 AA; 50119 MW; 4A341994FD28ADE7 CRC64;
MLLTLTTTHQ PATDLGHLLH KHPDRAQEFR TSAGTAHVFY PRADEQETTV ALLLEVDPVA
LVRGPGSTLT QYVNDRPYVA GSLFTVALGS VFRTAMNGRS QSRAELAATP IPLRVHVPVL
PFALVERLFT PLGWDVEVEP IALGDGTDSR YAAVTLTGAL RLSAALKHLY VLLPVLDGSK
HYWVDSDEVE KLLRAGDGWL ADHPDRELIT TRYLARKKPL VQSALARLAD LDDVEPEELD
NALAEPTIAQ AEPKVSLAVQ RRDAVVAALK AAGARRVLDL GCGGGALLRA LVQVPEFTEI
HGVDVSAKAL QEAARKLRLD RMSDRQRQRV VLRQSSLTYA DPALAGYDAA VLMEVVEHLD
PVRLPALEHS VFVVARPRTV LVTTPNVEYN ALFETLPAGR LRHNDHRFEW TRAEFRAWAT
GVAERRGYTV SFEPIGPEDP ALGAPTQMAV FVVGEQD
//
