ID G2HHU4_PANTR Unreviewed; 393 AA.
AC G2HHU4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Small RNA 2'-O-methyltransferase {ECO:0000256|ARBA:ARBA00021330};
DE EC=2.1.1.386 {ECO:0000256|ARBA:ARBA00035025};
DE AltName: Full=HEN1 methyltransferase homolog 1 {ECO:0000256|ARBA:ARBA00029981};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:BAK63302.1};
RN [1] {ECO:0000313|EMBL:BAK63302.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:BAK63302.1};
RX PubMed=21484476; DOI=10.1007/s10142-011-0220-9;
RA Kim R.N., Kim D.W., Choi S.H., Chae S.H., Nam S.H., Kim D.W., Kim A.,
RA Kang A., Park K.H., Lee Y.S., Hirai M., Suzuki Y., Sugano S., Hashimoto K.,
RA Kim D.S., Park H.S.;
RT "Major chimpanzee-specific structural changes in sperm development-
RT associated genes.";
RL Funct. Integr. Genomics 11:507-517(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK306308; BAK63302.1; -; mRNA.
DR RefSeq; NP_001267230.1; NM_001280301.1.
DR AlphaFoldDB; G2HHU4; -.
DR GeneID; 469399; -.
DR KEGG; ptr:469399; -.
DR CTD; 113802; -.
DR OrthoDB; 2735228at2759; -.
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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR026610; Hen1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR21404; HEN1; 1.
DR PANTHER; PTHR21404:SF3; SMALL RNA 2'-O-METHYLTRANSFERASE; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
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 REGION 286..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 44511 MW; 3E4A71260D6975A8 CRC64;
MEENNLQCSS VVDGNFEEVP RETAIQFKPP LYRQRYQFVK NLVDQHEPKK VADLGCGDTS
LLRLLKVNPC IELLVGVDIN EDKLRWRGDS LAPFLGDFLK PRDLNLTITL YHGSVVERDS
RLLGFDLITC IELIEHLDSG DLARFPEVVF GYLSPSMIVI STPNSEFNPL FPSVTLRDSD
HKFEWTRMEF QTWALYVANR YDYSVEFTGV GEPPAGAENV GYCTQIGIFR KNGGKATESC
LSEQLDQHVY KAVFTTSYPS LQQERFFKLV LVNEVSQQVE SLRVSHLPRR KEQAGERGDK
PKDIGGSKAP VPCFGPVFTE VEKAKIENSP TPFCVGDKFF VPLQRLLAYP KLNRLCANEE
MMRSVIADPI PLSSDGSAVV ADLRNYFDEQ FEF
//
