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Database: UniProt
Entry: D7MFH1_ARALL
LinkDB: D7MFH1_ARALL
Original site: D7MFH1_ARALL 
ID   D7MFH1_ARALL            Unreviewed;       943 AA.
AC   D7MFH1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Small RNA 2'-O-methyltransferase {ECO:0000256|ARBA:ARBA00021330};
DE            EC=2.1.1.386 {ECO:0000256|ARBA:ARBA00035025};
GN   ORFNames=ARALYDRAFT_492795 {ECO:0000313|EMBL:EFH44128.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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; GL348719; EFH44128.1; -; Genomic_DNA.
DR   RefSeq; XP_002867869.1; XM_002867823.1.
DR   AlphaFoldDB; D7MFH1; -.
DR   STRING; 81972.D7MFH1; -.
DR   EnsemblPlants; fgenesh2_kg.7__2228__AT4G20910.1; fgenesh2_kg.7__2228__AT4G20910.1; fgenesh2_kg.7__2228__AT4G20910.1.
DR   GeneID; 9303941; -.
DR   Gramene; fgenesh2_kg.7__2228__AT4G20910.1; fgenesh2_kg.7__2228__AT4G20910.1; fgenesh2_kg.7__2228__AT4G20910.1.
DR   KEGG; aly:9303941; -.
DR   eggNOG; KOG1045; Eukaryota.
DR   HOGENOM; CLU_001342_0_0_1; -.
DR   OrthoDB; 2735228at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblPlants.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblPlants.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0010589; P:leaf proximal/distal pattern formation; IEA:EnsemblPlants.
DR   GO; GO:0010305; P:leaf vascular tissue pattern formation; IEA:EnsemblPlants.
DR   GO; GO:0035196; P:miRNA processing; IEA:EnsemblPlants.
DR   GO; GO:0035279; P:miRNA-mediated gene silencing by mRNA destabilization; IEA:EnsemblPlants.
DR   GO; GO:0009909; P:regulation of flower development; IEA:EnsemblPlants.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0009616; P:RNAi-mediated antiviral immune response; IEA:EnsemblPlants.
DR   GO; GO:0010093; P:specification of floral organ identity; IEA:EnsemblPlants.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR026610; Hen1.
DR   InterPro; IPR040870; HEN1_dsRBD2.
DR   InterPro; IPR040813; Hen1_Lam_C.
DR   InterPro; IPR006630; La_HTH.
DR   InterPro; IPR025714; Methyltranfer_dom.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR21404; HEN1; 1.
DR   PANTHER; PTHR21404:SF3; SMALL RNA 2'-O-METHYLTRANSFERASE; 1.
DR   Pfam; PF17842; dsRBD2; 1.
DR   Pfam; PF18441; Hen1_Lam_C; 1.
DR   Pfam; PF21224; Hen1_LCD; 1.
DR   Pfam; PF13847; Methyltransf_31; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS50961; HTH_LA; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00332};
KW   RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          93..204
FT                   /note="HTH La-type RNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50961"
FT   REGION          284..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..597
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..860
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   943 AA;  104241 MW;  4D9A16260FD12B86 CRC64;
     MAGGGKHTPT PKAIIHQKFG AKASYRVEEV NDSSQSGCPG LAIPQKGPCL YRCHLQLPDF
     SVVSNVFKKK KDSEQSAAEL ALEKLGIRPQ NDDLTVDEAW DEIVGRIKYI FSDEFLSAEH
     PLGAHLRAAL RRDGERCGSV PVSVIATFDA KINSRCKIID PSVESDPFLA ISYVMKASAK
     LSDYIVVSQH ALRRKNAYPS EIVEALATHV SDSLHRREVA AVYIPCIDEE VVELDTLYIS
     SDRHYLDSIA ERLGLKDGSQ VMISSRTFGK ASCGSECRLY SDIPKKSSDN SSEASGSSNE
     DSSQIKKSRN ARASYICGQD IHGDAILASV GYRWKSDDLN YDDVTVNSFY RICCGMSPNG
     IYKISRQALI AAQLPFSFTT KSNWRGPLPR EILCLFCHQH RLAEPIISSS TAPVKSLSDI
     FRSHKKLKVS GVDDANENLS REKEDTPGLG HGFRCEVKIF TKSQDLVLEC SPRKFYEKEN
     DAIQNASLRA LLWFSKFFAD LDVDGEQPCD TDDDQDIKSP SPNVFAAPPI SQNEHSSESK
     TTNVLSAEKH VQSITNGSVV SICYSLSLAV DSEDSSDGES PREDIESNED MESEGDAEYS
     ANCEPSIDLI ESNEEIEFEV GTGSMNPHIE SAVTQMTVGE YSSFSITPPD AAEALILAVA
     SDTVRIRSLL SERPSLNYSI LLLGVKGPSE ERMEAAYFKP PLSKQRVEYA LKHIRESSAS
     TLVDFGCGSG SLLDSLLDYP TSLQTIIGVD ISPKGLARAA KMLHIKLNKE ACNVKSATLY
     DGSILEFDSR LHDVDIGTCL EVIEHMEEDQ ACEFGEKVLS LFHPKLLIVS TPNYEFNTIL
     QRSTSETQEE DKSGSQLPKF RNHDHKFEWT REQFNNWASN LAKRHNYGVE FSGVGGSGEV
     EPGFASQIAV FRREASSVEN VAESSMQPYK VIWEWKKDGD KKD
//
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