MET16_CAEBR
ID MET16_CAEBR Reviewed; 481 AA.
AC Q61J97; A8X9V8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=U6 small nuclear RNA (adenine-(43)-N(6))-methyltransferase;
DE EC=2.1.1.346 {ECO:0000250|UniProtKB:O42662, ECO:0000250|UniProtKB:Q86W50};
DE AltName: Full=N6-adenosine-methyltransferase mett-10 {ECO:0000305};
DE EC=2.1.1.348 {ECO:0000250|UniProtKB:Q09357};
GN Name=mett-10 {ECO:0000312|WormBase:CBG09879};
GN ORFNames=CBG09879 {ECO:0000312|WormBase:CBG09879};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: RNA N6-methyltransferase that methylates adenosine residues
CC at the N(6) position of a subset of RNAs and is involved in S-adenosyl-
CC L-methionine homeostasis by regulating splicing of S-adenosylmethionine
CC synthase transcripts (sams-3, sams-4 and sams-5). Able to N6-methylate
CC a subset of mRNAs containing the 5'UACAGAAAC-3' nonamer sequence. Plays
CC a key role in S-adenosyl-L-methionine homeostasis: under rich-diet
CC conditions, catalyzes N6-methylation of S-adenosylmethionine synthase
CC mRNAs (sams-3, sams-4 and sams-5), directly inhibiting splicing and
CC protein production of S-adenosylmethionine synthase. In addition to
CC mRNAs, also able to mediate N6-methylation of U6 small nuclear RNA (U6
CC snRNA). Required for gamete production, inhibiting germ cell
CC proliferative fate and ensuring germ cell meiotic development. Also
CC promotes progression of the mitotic cell cycle in those germ cells that
CC continue to proliferate. Plays a role in the development of the vulva,
CC somatic gonad and embryo. {ECO:0000250|UniProtKB:Q09357}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(6)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55584, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.348;
CC Evidence={ECO:0000250|UniProtKB:Q09357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55585;
CC Evidence={ECO:0000250|UniProtKB:Q09357};
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:0000250|UniProtKB:Q09357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52809;
CC Evidence={ECO:0000250|UniProtKB:Q09357};
CC -!- SUBUNIT: Self-associates. Interacts with dlc-1; the interaction is
CC direct, and is required for nuclear localization of mett-10.
CC {ECO:0000250|UniProtKB:Q09357}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q09357}.
CC Note=Accumulates in nuclei as cells enter meiosis. During meiotic
CC prophase, expression is predominantly nuclear, but does not co-localize
CC with DNA. Recruited to the nucleus by dlc-1, a component of the dynein
CC complex. {ECO:0000250|UniProtKB:Q09357}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL16/RlmF
CC family. {ECO:0000305}.
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DR EMBL; HE601459; CAP29423.1; -; Genomic_DNA.
DR RefSeq; XP_002641577.1; XM_002641531.1.
DR AlphaFoldDB; Q61J97; -.
DR SMR; Q61J97; -.
DR STRING; 6238.CBG09879; -.
DR GeneID; 8583568; -.
DR KEGG; cbr:CBG_09879; -.
DR CTD; 8583568; -.
DR WormBase; CBG09879; CBP40153; WBGene00031392; Cbr-mett-10.
DR eggNOG; KOG2912; Eukaryota.
DR HOGENOM; CLU_027534_0_0_1; -.
DR InParanoid; Q61J97; -.
DR OMA; TEFCQGH; -.
DR OrthoDB; 1358504at2759; -.
DR Proteomes; UP000008549; Chromosome III.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0052907; F:23S rRNA (adenine(1618)-N(6))-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell cycle; Cell division; Meiosis; Methyltransferase; Mitosis; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..481
FT /note="U6 small nuclear RNA (adenine-(43)-N(6))-
FT methyltransferase"
FT /id="PRO_0000310772"
FT BINDING 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86W50"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86W50"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86W50"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86W50"
FT BINDING 184
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q86W50"
SQ SEQUENCE 481 AA; 54143 MW; 0354435BBF934AE6 CRC64;
MAQGNEMHPR NPYRDKPPDF KALAIEYPEF RKFCQYVSNG KVTLDFRKDA AVRCLTQTLL
KKDFSLNVNL PAGHLVPRVP QKLNYCLLID DILQANSITS NVVGIDIGTG TSCIHALIGA
RHFGWKFVAT DGDENSVQVA HENVARNEMG DSICVVHVNP AVKTVLMDVI NSMPDSEFSF
CMCNPPFFEK SDKEERFCEE PSLSNETYSN NFDFDMRSAP HSETIASSAE LYVEGGEVAF
VNRIIDDSVC LRDRIKFYTT MIGRKSSLKP LLQRLERFGE NVKFLVHPLN QGKTKRWMLA
WTFAKEMTLN TALKNSSISF QCPKPGLVKL MQEISRLGGR WSQEQPSVLV AEFKSVTWTN
QRARRKANAL LFENSAKRAR WNTSSVACEA MMGNGDGKDS YTNSGNFVYS ESFKTSDPAA
VETSSQAYFP LPSGVTPRPI VKLRIQVDPD DKCDTLSFEL ISGAKQHLHQ IVQYLKNLLC
R
