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Small RNA 2'-O-methyltransferase (EC 2.1.1.n8) (HEN1 methyltransferase homolog 1)

 HENMT_TETTS             Reviewed;         423 AA.
Q230X8; B6ETG8;
05-APR-2011, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 3.
05-JUL-2017, entry version 47.
RecName: Full=Small RNA 2'-O-methyltransferase;
EC=2.1.1.n8 {ECO:0000269|PubMed:19240163};
AltName: Full=HEN1 methyltransferase homolog 1;
Name=HEN1; ORFNames=TTHERM_00433810;
Tetrahymena thermophila (strain SB210).
Eukaryota; Alveolata; Ciliophora; Intramacronucleata;
Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
Tetrahymena.
NCBI_TaxID=312017;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, INTERACTION WITH TWI1, AND DISRUPTION PHENOTYPE.
STRAIN=B2086 x CU428;
PubMed=19240163; DOI=10.1261/rna.1455509;
Kurth H.M., Mochizuki K.;
"2'-O-methylation stabilizes Piwi-associated small RNAs and ensures
DNA elimination in Tetrahymena.";
RNA 15:675-685(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SB210;
PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M.,
Sun L., Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E.,
Wang Y., Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K.,
Weinberg Z., Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C.,
Gorovsky M.A., Keeling P.J., Waller R.F., Patron N.J., Cherry J.M.,
Stover N.A., Krieger C.J., del Toro C., Ryder H.F., Williamson S.C.,
Barbeau R.A., Hamilton E.P., Orias E.;
"Macronuclear genome sequence of the ciliate Tetrahymena thermophila,
a model eukaryote.";
PLoS Biol. 4:1620-1642(2006).
-!- FUNCTION: Methyltransferase that adds a 2'-O-methyl group at the
3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are
generated by a Dicer-independent mechanism and are primarily
derived from transposons and other repeated sequence elements.
This probably protects the 3'-end of piRNAs from uridylation
activity and subsequent degradation. Required for programmed DNA
elimination. {ECO:0000269|PubMed:19240163}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + small RNA = S-
adenosyl-L-homocysteine + small RNA containing a 3'-terminal 2'-O-
methylnucleotide. {ECO:0000269|PubMed:19240163}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9C5Q8};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:Q9C5Q8};
-!- SUBUNIT: Interacts with TWI1. {ECO:0000269|PubMed:19240163}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19240163}.
Note=Localizes to the macronucleus.
-!- DISRUPTION PHENOTYPE: Defects in programmed DNA elimination, and
inefficient production of sexual progeny due to reduction in the
level and length of piRNAs. {ECO:0000269|PubMed:19240163}.
-!- SIMILARITY: Belongs to the methyltransferase superfamily. HEN1
family. {ECO:0000305}.
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EMBL; FM199973; CAQ86608.1; -; mRNA.
EMBL; GG662532; EAR91161.3; -; Genomic_DNA.
RefSeq; XP_001011406.3; XM_001011406.4.
ProteinModelPortal; Q230X8; -.
SMR; Q230X8; -.
STRING; 5911.EAR91161; -.
EnsemblProtists; EAR91161; EAR91161; TTHERM_00433810.
GeneID; 7840569; -.
KEGG; tet:TTHERM_00433810; -.
InParanoid; Q230X8; -.
KO; K20798; -.
Proteomes; UP000009168; Unassembled WGS sequence.
GO; GO:0031039; C:macronucleus; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0008173; F:RNA methyltransferase activity; IDA:UniProtKB.
GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
GO; GO:0034587; P:piRNA metabolic process; IDA:UniProtKB.
GO; GO:0031049; P:programmed DNA elimination; IMP:UniProtKB.
GO; GO:0001510; P:RNA methylation; IDA:UniProtKB.
InterPro; IPR026610; Hen1.
InterPro; IPR029063; SAM-dependent_MTases.
PANTHER; PTHR21404; PTHR21404; 1.
SUPFAM; SSF53335; SSF53335; 1.
1: Evidence at protein level;
Complete proteome; Metal-binding; Methyltransferase; Nucleus;
Reference proteome; RNA-binding; RNA-mediated gene silencing;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 423 Small RNA 2'-O-methyltransferase.
/FTId=PRO_0000406962.
METAL 124 124 Magnesium.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 127 127 Magnesium.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 128 128 Magnesium; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9C5Q8}.
METAL 177 177 Magnesium; via tele nitrogen.
{ECO:0000250|UniProtKB:Q9C5Q8}.
BINDING 65 65 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q9C5Q8}.
BINDING 104 104 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:Q9C5Q8}.
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


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