HENMT_SCHPO
ID HENMT_SCHPO Reviewed; 378 AA.
AC Q9UST9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Small RNA 2'-O-methyltransferase;
DE EC=2.1.1.n8;
DE AltName: Full=HEN1 methyltransferase homolog;
GN ORFNames=SPBC336.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end
CC of small RNAs. {ECO:0000250}.
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.n8;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB58157.1; -; Genomic_DNA.
DR PIR; T40243; T40243.
DR RefSeq; NP_596125.1; NM_001022043.2.
DR AlphaFoldDB; Q9UST9; -.
DR SMR; Q9UST9; -.
DR BioGRID; 276783; 25.
DR STRING; 4896.SPBC336.05c.1; -.
DR PaxDb; Q9UST9; -.
DR EnsemblFungi; SPBC336.05c.1; SPBC336.05c.1:pep; SPBC336.05c.
DR GeneID; 2540251; -.
DR KEGG; spo:SPBC336.05c; -.
DR PomBase; SPBC336.05c; -.
DR VEuPathDB; FungiDB:SPBC336.05c; -.
DR eggNOG; KOG1045; Eukaryota.
DR HOGENOM; CLU_738011_0_0_1; -.
DR InParanoid; Q9UST9; -.
DR OMA; FERICSP; -.
DR PhylomeDB; Q9UST9; -.
DR PRO; PR:Q9UST9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; ISO:PomBase.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; ISO:PomBase.
DR GO; GO:0034587; P:piRNA metabolic process; IBA:GO_Central.
DR GO; GO:0030422; P:siRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026610; Hen1.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR21404; PTHR21404; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW RNA-binding; RNA-mediated gene silencing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..378
FT /note="Small RNA 2'-O-methyltransferase"
FT /id="PRO_0000343141"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 378 AA; 43827 MW; F7C3AC50CAF7383E CRC64;
MGVSSFYPPL HVQRRRKLFK ILQGGFPVRS LLDIGCGDAR FLSYLVPCND QVPIEFLAGI
DINEQSIERA TEALQVRTED FLQLRWRPLH IELLLGNIKD FTHYKHVDAV VASEFIEHCQ
VAEILAFEKL VFGNLKPNVC VVSTPNFEFN TIFEKLSTLT SSISSRTSTN FRHPEHVFEW
DRKEFAKWAY KICKRYPEYT VEFTGCGLLN DLIDGDDLLH FRPSSTYGFC TQIAVFHQSK
NNAASHCFLK DQNSSILLYK KITYPFMEQL FPPTVQQFMN LLKKAFFDHL FGRHCLLLFQ
VIAGKCALSV KLPFLFIWES SPLIRHAFHY DDSIYLSYCP ELKKSKHKGI ALANSFSFRI
AKVLKKSRIF IITFHHYV
