ID A0A1V2QRI0_9PSEU Unreviewed; 450 AA.
AC A0A1V2QRI0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Small RNA 2'-O-methyltransferase {ECO:0000256|ARBA:ARBA00021330};
DE EC=2.1.1.386 {ECO:0000256|ARBA:ARBA00035025};
GN ORFNames=ALI22I_11350 {ECO:0000313|EMBL:ONI90705.1};
OS Saccharothrix sp. ALI-22-I.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI90705.1, ECO:0000313|Proteomes:UP000188617};
RN [1] {ECO:0000313|EMBL:ONI90705.1, ECO:0000313|Proteomes:UP000188617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI90705.1,
RC ECO:0000313|Proteomes:UP000188617};
RX PubMed=28087533;
RA Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA Kuske C.R.;
RT "Polysaccharide degradation capability of Actinomycetales soil isolates
RT from a semi-arid grassland of the Colorado Plateau.";
RL Appl. Environ. Microbiol. 0:0-0(2017).
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:ONI90705.1}.
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DR EMBL; MTQP01000051; ONI90705.1; -; Genomic_DNA.
DR RefSeq; WP_077005431.1; NZ_MTQP01000051.1.
DR AlphaFoldDB; A0A1V2QRI0; -.
DR STRING; 1933778.ALI22I_11350; -.
DR OrthoDB; 626362at2; -.
DR Proteomes; UP000188617; 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:ONI90705.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000188617};
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:ONI90705.1}.
FT DOMAIN 1..229
FT /note="Hen1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12623"
FT DOMAIN 271..363
FT /note="Methyltransferase type 12"
FT /evidence="ECO:0000259|Pfam:PF08242"
SQ SEQUENCE 450 AA; 50019 MW; 64CB3687028C285D CRC64;
MLLTLTTTHR PATALSHLLH KHPERAQSFT TSSGTAHVFY PRADDEECTV ALLLEVDPVA
LVRGPGSTLT QYVNDRPYVA GSLLTVALGS VFRTAMSGRS KSHQDVAATP IPLTVRVPVL
PHRLVERLFT PLGWTTRIVP VPLGDGEDSR YADVTLTGTL TLSDALKHLY VLLPVLDGNK
HYWVSQDEVD KLLRAGEGWL GTHPDRELIT TRYLMRSRPL VQSALSRLAD VEELEPEELD
NALTEPKVSL AVQRREAVLD QLKQAGARTV LDLGCGGGAL LRALLEHPEF THIHGVDVSS
RALATAERKL HVDRMSDRQR ARLTLRQSSL TYADPALKGY DAAVLMEVVE HLDPDRLPAL
EHSVFVVARP RTVLVTTPNV EYNALFETLP ENQHRHSDHR FEWTRAEFED WTNGVAQRRG
YTVRHLPIGP VDDERGAPTQ LAVFVVGDEN
//
