MTL16_SCHPO
ID MTL16_SCHPO Reviewed; 385 AA.
AC O42662;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase;
DE EC=2.1.1.346 {ECO:0000305|PubMed:28525753};
GN ORFNames=SPAC27D7.08c;
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).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28525753; DOI=10.1016/j.cell.2017.05.003;
RA Pendleton K.E., Chen B., Liu K., Hunter O.V., Xie Y., Tu B.P., Conrad N.K.;
RT "The U6 snRNA m(6)A methyltransferase METTL16 regulates SAM synthetase
RT intron retention.";
RL Cell 169:824-835(2017).
CC -!- FUNCTION: RNA N6-methyltransferase that mediates N6-methylation of
CC adenine of U6 small nuclear RNA (U6 snRNA).
CC {ECO:0000305|PubMed:28525753}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine in U6 snRNA + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyladenosine in U6 snRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:52808, Rhea:RHEA-COMP:13573, Rhea:RHEA-COMP:13574,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.346;
CC Evidence={ECO:0000305|PubMed:28525753};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL16/RlmF
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAA15827.2; -; Genomic_DNA.
DR PIR; T38441; T38441.
DR RefSeq; NP_594614.1; NM_001020042.2.
DR AlphaFoldDB; O42662; -.
DR SMR; O42662; -.
DR BioGRID; 278696; 4.
DR STRING; 4896.SPAC27D7.08c.1; -.
DR PaxDb; O42662; -.
DR EnsemblFungi; SPAC27D7.08c.1; SPAC27D7.08c.1:pep; SPAC27D7.08c.
DR GeneID; 2542223; -.
DR KEGG; spo:SPAC27D7.08c; -.
DR PomBase; SPAC27D7.08c; -.
DR VEuPathDB; FungiDB:SPAC27D7.08c; -.
DR eggNOG; KOG2912; Eukaryota.
DR HOGENOM; CLU_027534_0_1_1; -.
DR InParanoid; O42662; -.
DR OMA; HQGRYDF; -.
DR PhylomeDB; O42662; -.
DR PRO; PR:O42662; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0052907; F:23S rRNA (adenine(1618)-N(6))-methyltransferase activity; ISO:PomBase.
DR GO; GO:0120048; F:U6 snRNA (adenine-(43)-N(6))-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0070475; P:rRNA base methylation; ISO:PomBase.
DR GO; GO:0120049; P:snRNA (adenine-N6)-methylation; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR017182; METTL16/PsiM.
DR InterPro; IPR010286; METTL16/RlmF.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13393; PTHR13393; 1.
DR Pfam; PF05971; Methyltransf_10; 1.
DR PIRSF; PIRSF037350; Mtase_ZK1128_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..385
FT /note="U6 small nuclear RNA (adenine-(43)-N(6))-
FT methyltransferase"
FT /id="PRO_0000339418"
FT BINDING 54
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86W50"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86W50"
FT BINDING 106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86W50"
FT BINDING 155
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86W50"
SQ SEQUENCE 385 AA; 44422 MW; B60192AE43E3CD05 CRC64;
MPIYILIERS VKNGRIDFWN EDAIRTLGKA ILDRDYSLRV EFPENRLCPM VPNRATYIRY
IHDLLSSTSG QKDKKRIIGL DIGTGASCIY PLLGCRMYSY DFVGTEIDKF SFETAKSNIL
QNNMESQIKI VLRSKQDCLL PDTEGMEEFT FVMCNPPFYE HEEDFINFKQ NPPSGVCTGV
YHEMVTEGGE VGFANKILTE SKKRKGIQWY TCMFGKKSSV PAVVDKLREQ NISNYGIYEL
ALGKTKRWII CWSFQAMRPH NELIRPSSTS LSKYFPHKVL QNWTLDPELC AQIDDILQKF
LDDNKIPWSK KGSVLEISTK SITWSRKARR ISKSQTSVSS LEGQMKCELN VIDNQLQCKW
IEGYDYNVYE SFCSALARAL RDNKK
