ID   HENMT_TETTS             Reviewed;         423 AA.
AC   Q230X8; B6ETG8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Small RNA 2'-O-methyltransferase;
DE            EC=2.1.1.n8 {ECO:0000269|PubMed:19240163};
DE   AltName: Full=HEN1 methyltransferase homolog 1;
GN   Name=HEN1; ORFNames=TTHERM_00433810;
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, INTERACTION WITH TWI1, AND DISRUPTION PHENOTYPE.
RC   STRAIN=B2086 x CU428;
RX   PubMed=19240163; DOI=10.1261/rna.1455509;
RA   Kurth H.M., Mochizuki K.;
RT   "2'-O-methylation stabilizes Piwi-associated small RNAs and ensures DNA
RT   elimination in Tetrahymena.";
RL   RNA 15:675-685(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210;
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
CC   -!- FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the 3'-end
CC       of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a
CC       Dicer-independent mechanism and are primarily derived from transposons
CC       and other repeated sequence elements. This probably protects the 3'-end
CC       of piRNAs from uridylation activity and subsequent degradation.
CC       Required for programmed DNA elimination. {ECO:0000269|PubMed:19240163}.
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         Evidence={ECO:0000269|PubMed:19240163};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9C5Q8};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9C5Q8};
CC   -!- SUBUNIT: Interacts with TWI1. {ECO:0000269|PubMed:19240163}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19240163}.
CC       Note=Localizes to the macronucleus.
CC   -!- DISRUPTION PHENOTYPE: Defects in programmed DNA elimination, and
CC       inefficient production of sexual progeny due to reduction in the level
CC       and length of piRNAs. {ECO:0000269|PubMed:19240163}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1 family.
CC       {ECO:0000305}.
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DR   EMBL; FM199973; CAQ86608.1; -; mRNA.
DR   EMBL; GG662532; EAR91161.3; -; Genomic_DNA.
DR   RefSeq; XP_001011406.3; XM_001011406.4.
DR   AlphaFoldDB; Q230X8; -.
DR   SMR; Q230X8; -.
DR   STRING; 5911.EAR91161; -.
DR   PRIDE; Q230X8; -.
DR   EnsemblProtists; EAR91161; EAR91161; TTHERM_00433810.
DR   GeneID; 7840569; -.
DR   KEGG; tet:TTHERM_00433810; -.
DR   eggNOG; KOG1045; Eukaryota.
DR   HOGENOM; CLU_649718_0_0_1; -.
DR   InParanoid; Q230X8; -.
DR   OrthoDB; 789470at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0031039; C:macronucleus; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0090486; F:small RNA 2'-O-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0034587; P:piRNA metabolic process; IDA:UniProtKB.
DR   GO; GO:0031049; P:programmed DNA elimination; IMP:UniProtKB.
DR   GO; GO:0001510; P:RNA methylation; IDA:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR026610; Hen1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR21404; PTHR21404; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Magnesium; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW   RNA-binding; RNA-mediated gene silencing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..423
FT                   /note="Small RNA 2'-O-methyltransferase"
FT                   /id="PRO_0000406962"
FT   BINDING         65
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT   BINDING         104
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT   BINDING         127
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C5Q8"
SQ   SEQUENCE   423 AA;  49946 MW;  4F13D9FD78417675 CRC64;
     MIEAYETDVF MDPIGMKVWE KRHQYVATKL SALNCKRVLD MGTNTCKLIQ RLSRSLQFTQ
     IDGLDIDGQL LETQGIQNAK PDLIQNQYAS MRDHQLVVNL YQGSALNKIQ HLKDQQYDAV
     ILVELIEHLQ VEDVFLIEQN LFGFLRPQFV IVTTPNSDFN VYFNFKEQGV LFRDKDHKFE
     WSQNQFQIWA QKVCQNYGYK VIELTGVGEH KTEGTKNGFC TQIVVFEKDT QQEKYLNFAF
     FNLQEGEIRQ VCQILYPFES KEQHFQREVV DSIRYILHIT DKQNQFEDGS YQNYTTLSRI
     MQNHSISSNW QIQGDYFKLK TYIQNISEFL VHENQFNFQE SFVTLNYQAQ MEDEENEDQL
     ESDSENVKMQ QQQYYFSNDN CFSTKDTTYS SFSTADNLFS QKIQLGQQQM ALEEIELEDT
     IDY