ID A0A2K8PDU7_STRLA Unreviewed; 507 AA.
AC A0A2K8PDU7;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Small RNA 2'-O-methyltransferase {ECO:0000256|ARBA:ARBA00021330};
DE EC=2.1.1.386 {ECO:0000256|ARBA:ARBA00035025};
GN ORFNames=SLAV_10225 {ECO:0000313|EMBL:ATZ23913.1}, SLLC_08255
GN {ECO:0000313|EMBL:QUQ53744.1};
OS Streptomyces lavendulae subsp. lavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=58340 {ECO:0000313|EMBL:ATZ23913.1, ECO:0000313|Proteomes:UP000231791};
RN [1] {ECO:0000313|EMBL:ATZ23913.1, ECO:0000313|Proteomes:UP000231791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 3239 {ECO:0000313|EMBL:ATZ23913.1,
RC ECO:0000313|Proteomes:UP000231791};
RA Busche T., Novakova R., Al'Dilaimi A., Homerova D., Feckova L.,
RA Rezuchova B., Mingyar E., Csolleiova D., Bekeova C., Winkler A.,
RA Sevcikova B., Kalinowski J., Kormanec J., Ruckert C.;
RT "Complete genome sequence of Streptomyces lavendulae subsp. lavendulae CCM
RT 3239 (formerly 'Streptomyces aureofaciens CCM 3239'), the producer of the
RT angucycline-type antibiotic auricin.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QUQ53744.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Del-LP {ECO:0000313|EMBL:QUQ53744.1};
RA Novakova R., Ruckert C., Knirschova R., Feckova L., Busche T.,
RA Csolleiova D., Homerova D., Rezuchova B., Javorova R., Sevcikova B.,
RA Kalinowski J., Kormanec J.;
RT "The linear plasmid pSA3239 is essential for the replication of the
RT Streptomyces lavendulae subsp. lavendulae CCM 3239 chromosome.";
RL Submitted (APR-2021) 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; CP024985; ATZ23913.1; -; Genomic_DNA.
DR EMBL; CP073778; QUQ53744.1; -; Genomic_DNA.
DR RefSeq; WP_030238266.1; NZ_JOEW01000040.1.
DR AlphaFoldDB; A0A2K8PDU7; -.
DR GeneID; 82164043; -.
DR KEGG; slx:SLAV_10225; -.
DR OrthoDB; 626362at2; -.
DR Proteomes; UP000231791; Chromosome.
DR Proteomes; UP000676025; Chromosome.
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:QUQ53744.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231791};
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:QUQ53744.1};
KW Ubiquinone {ECO:0000313|EMBL:QUQ53744.1}.
FT DOMAIN 1..251
FT /note="Hen1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12623"
FT DOMAIN 305..394
FT /note="Methyltransferase type 12"
FT /evidence="ECO:0000259|Pfam:PF08242"
FT REGION 483..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 55391 MW; EB9C3077F80E0DCD CRC64;
MFLTISTTGT PERPATDLGF LLHKHPGKAQ EFTTSHGTAH VFYPEATAER CTAALLLEVD
PVALVRRSQG KGKGRGGAPD AALAQYVNDR PYAASSLFAV ALGKVFRSAL AGTCAARPEL
PGRPRPLRVE LPALPARGGA DLVRRLFGPL GWDSVRTEPV ALDERFPEWG DSRYVRLVLE
GELKLDDALR QLYVLLPVLD DAKHYWIAPD EVDKLLRAGD GWLAAHPEHA LITARYLARH
KRLTQDAMER LELARLAEAD GSEAGELDDA AEEQPDDTQR SVPLAVRRRE AILAALRSAG
AARVLDLGCG QGQLVQALLK DPSFTEIVGV DVSVRALATA ARRLRLERMG ERQSSRVTLL
QGSLAYTDKR LAGYDAAVLS EVVEHLDLPR LPALEYAVFG AARPRTVLVT TPNVEYNVRW
ESLPAGHVRH RDHRFEWNRE EFRAWAGEVA ARYGYTVVYA PVGEDDPEVG PPTQMAVFTA
AATDFPSATE TPSATETTDT PKEGEAA
//
