METL5_CAEEL
ID METL5_CAEEL Reviewed; 214 AA.
AC Q18511;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=rRNA N6-adenosine-methyltransferase metl-5;
DE EC=2.1.1.- {ECO:0000305|PubMed:33357433};
DE AltName: Full=Methyltransferase-like protein 5 {ECO:0000305};
GN Name=metl-5 {ECO:0000303|PubMed:33357433, ECO:0000312|WormBase:C38D4.9};
GN ORFNames=C38D4.9 {ECO:0000312|WormBase:C38D4.9};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=33357433; DOI=10.1016/j.celrep.2020.108544;
RA Rong B., Zhang Q., Wan J., Xing S., Dai R., Li Y., Cai J., Xie J., Song Y.,
RA Chen J., Zhang L., Yan G., Zhang W., Gao H., Han J.J., Qu Q., Ma H.,
RA Tian Y., Lan F.;
RT "Ribosome 18S m6A methyltransferase METTL5 promotes translation initiation
RT and breast cancer cell growth.";
RL Cell Rep. 33:108544-108544(2020).
CC -!- FUNCTION: Catalytic subunit of a heterodimer with TRMT112/C04H5.1,
CC which specifically methylates the 6th position of adenine in position
CC 1717 of 18S rRNA. {ECO:0000269|PubMed:33357433}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine in rRNA + S-adenosyl-L-methionine = H(+) + N(6)-
CC methyladenosine in rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:58728, Rhea:RHEA-COMP:15198, Rhea:RHEA-COMP:15199,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449;
CC Evidence={ECO:0000305|PubMed:33357433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58729;
CC Evidence={ECO:0000305|PubMed:33357433};
CC -!- SUBUNIT: Heterodimer; heterodimerizes with TRMT112/C04H5.1.
CC {ECO:0000250|UniProtKB:Q9NRN9}.
CC -!- DISRUPTION PHENOTYPE: Worms are viable and do not display obvious
CC developmental defects; they however exhibit significantly longer
CC lifespan and heat resistance (PubMed:33357433). Cells show reduced N6-
CC methylation of adenine(1717) in 18S rRNA (PubMed:33357433).
CC {ECO:0000269|PubMed:33357433}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC {ECO:0000305}.
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DR EMBL; BX284603; CAA86320.1; -; Genomic_DNA.
DR PIR; T19827; T19827.
DR RefSeq; NP_497990.1; NM_065589.4.
DR AlphaFoldDB; Q18511; -.
DR SMR; Q18511; -.
DR DIP; DIP-24672N; -.
DR IntAct; Q18511; 1.
DR STRING; 6239.C38D4.9; -.
DR EPD; Q18511; -.
DR PaxDb; Q18511; -.
DR PeptideAtlas; Q18511; -.
DR EnsemblMetazoa; C38D4.9.1; C38D4.9.1; WBGene00008008.
DR GeneID; 175637; -.
DR KEGG; cel:CELE_C38D4.9; -.
DR UCSC; C38D4.9; c. elegans.
DR CTD; 175637; -.
DR WormBase; C38D4.9; CE00922; WBGene00008008; metl-5.
DR eggNOG; KOG3420; Eukaryota.
DR GeneTree; ENSGT00390000000227; -.
DR HOGENOM; CLU_074702_1_1_1; -.
DR InParanoid; Q18511; -.
DR OMA; DVVYSIH; -.
DR OrthoDB; 1528520at2759; -.
DR PhylomeDB; Q18511; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00008008; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008988; F:rRNA (adenine-N6-)-methyltransferase activity; IDA:WormBase.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0032056; P:positive regulation of translation in response to stress; IMP:WormBase.
DR GO; GO:0070475; P:rRNA base methylation; IDA:WormBase.
DR GO; GO:0031167; P:rRNA methylation; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..214
FT /note="rRNA N6-adenosine-methyltransferase metl-5"
FT /id="PRO_0000453465"
FT BINDING 25
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 28
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 106..107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
SQ SEQUENCE 214 AA; 23919 MW; 646A9B31A7BDFC4B CRC64;
MPDKKTLWML NELEGFEKPK IKLEQYATSS ELAVSMMEMI DETIGFEGKK LIDIGCGCGM
LMTTAATMYE LETVLGVDID DEALKICSRN LETAEVQDRC ELLQADILDP ESDLPRGTFD
VAVINPPFGT KNNAGIDMQF VQIGLQMVRP GGSVFSLHKS STRDYILKNA KKWDGVGAEC
CAEMRWQLPA TYKFHKQKAV DIAVDLIHFK KLDS
