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Database: UniProt
Entry: A0A1H7LQS9_9ACTN
LinkDB: A0A1H7LQS9_9ACTN
Original site: A0A1H7LQS9_9ACTN 
ID   A0A1H7LQS9_9ACTN        Unreviewed;       496 AA.
AC   A0A1H7LQS9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Small RNA 2'-O-methyltransferase {ECO:0000256|ARBA:ARBA00021330};
DE            EC=2.1.1.386 {ECO:0000256|ARBA:ARBA00035025};
GN   ORFNames=SAMN05660976_01645 {ECO:0000313|EMBL:SEL01266.1};
OS   Nonomuraea pusilla.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=46177 {ECO:0000313|EMBL:SEL01266.1, ECO:0000313|Proteomes:UP000198953};
RN   [1] {ECO:0000313|EMBL:SEL01266.1, ECO:0000313|Proteomes:UP000198953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43357 {ECO:0000313|EMBL:SEL01266.1,
RC   ECO:0000313|Proteomes:UP000198953};
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; FOBF01000003; SEL01266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7LQS9; -.
DR   STRING; 46177.SAMN05660976_01645; -.
DR   OrthoDB; 626362at2; -.
DR   Proteomes; UP000198953; 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:SEL01266.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198953};
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:SEL01266.1}.
FT   DOMAIN          1..242
FT                   /note="Hen1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12623"
FT   DOMAIN          320..411
FT                   /note="Methyltransferase type 12"
FT                   /evidence="ECO:0000259|Pfam:PF08242"
FT   REGION          244..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..265
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  54056 MW;  9717387D036A1669 CRC64;
     MLLTITTTSR PATDLGFLLH KHPERVQEFG GSYGTATVFY PEAGEDRCTA ALLLEVDPVA
     LVRSRGRNSP DFSLSQYVND RPYAASSLLA VALADVFRTA RAGRCAARPE LPGTPLPLEI
     RLPALPCRGG PELAERLFAP LGWQVSAESV PLDEGFPAWG ESRYVRLVLT GTLRLSDALN
     HLYVLLPVLD DGKHYWIAPD EVDKLVRAGE GWLGGHPERG LITRRYLGRR WSLARTALAR
     LAELGDETEE ELEPPVAEEA SPEETAADEA AAAGTAAEGA AGAPAEGEPG QERKPRSLSV
     LRREAVLGVL EELGAVSVAD LGCGQGELLA ALLARPRFAR VAGMDVSSMA LTIAARRLRL
     DRMPDAVRAR LTLFQGSLTY TDKRLRGYDA AVLMEVVEHV DPPRLAALEH VVFGHARPAH
     VVVTTPNVEY NVRYPFLTGL RHPDHRFEWT RAEFAAWAAR VAAEHGYEVA FRPVGDDDPE
     VGPPTQMGVF TRDQRS
//
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