METL5_DROME
ID METL5_DROME Reviewed; 213 AA.
AC Q8MSW4; Q9VVX7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=rRNA N6-adenosine-methyltransferase Mettl5;
DE EC=2.1.1.- {ECO:0000269|PubMed:32350990};
DE AltName: Full=Methyltransferase-like protein 5;
GN Name=Mettl5 {ECO:0000312|FlyBase:FBgn0036856};
GN ORFNames=CG9666 {ECO:0000312|FlyBase:FBgn0036856};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH CG12975.
RX PubMed=32350990; DOI=10.15252/embr.201949443;
RA Leismann J., Spagnuolo M., Pradhan M., Wacheul L., Vu M.A., Musheev M.,
RA Mier P., Andrade-Navarro M.A., Graille M., Niehrs C., Lafontaine D.L.,
RA Roignant J.Y.;
RT "The 18S ribosomal RNA m6 A methyltransferase Mettl5 is required for normal
RT walking behavior in Drosophila.";
RL EMBO Rep. 21:e49443-e49443(2020).
CC -!- FUNCTION: Catalytic subunit of a heterodimer with Trmt112/CG12975,
CC which specifically methylates the 6th position of adenine in 18S rRNA.
CC {ECO:0000269|PubMed:32350990}.
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:0000269|PubMed:32350990};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58729;
CC Evidence={ECO:0000269|PubMed:32350990};
CC -!- SUBUNIT: Heterodimer; heterodimerizes with Trmt112/CG12975.
CC {ECO:0000269|PubMed:32350990}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32350990}.
CC -!- TISSUE SPECIFICITY: Enriched in the brain.
CC {ECO:0000269|PubMed:32350990}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high level in early embryo.
CC Expression gradually decreases and remains low in the larval stages. A
CC mild increase is observed at metamorphosis, and this level remains
CC constant in the adult phase. {ECO:0000269|PubMed:32350990}.
CC -!- DISRUPTION PHENOTYPE: Flies are viable and fertile and do not display
CC obvious developmental defects (PubMed:32350990). They however show
CC impaired orientation in walking behavioral assays (PubMed:32350990).
CC {ECO:0000269|PubMed:32350990}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. PrmA family.
CC {ECO:0000305}.
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DR EMBL; AE014296; ACL83328.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49178.2; -; Genomic_DNA.
DR EMBL; AY118530; AAM49899.1; -; mRNA.
DR RefSeq; NP_001137973.1; NM_001144501.2.
DR RefSeq; NP_649098.2; NM_140841.3.
DR AlphaFoldDB; Q8MSW4; -.
DR SMR; Q8MSW4; -.
DR STRING; 7227.FBpp0074759; -.
DR PaxDb; Q8MSW4; -.
DR EnsemblMetazoa; FBtr0074991; FBpp0074759; FBgn0036856.
DR EnsemblMetazoa; FBtr0344454; FBpp0310826; FBgn0036856.
DR GeneID; 40096; -.
DR KEGG; dme:Dmel_CG9666; -.
DR UCSC; CG9666-RA; d. melanogaster.
DR FlyBase; FBgn0036856; Mettl5.
DR VEuPathDB; VectorBase:FBgn0036856; -.
DR eggNOG; KOG3420; Eukaryota.
DR GeneTree; ENSGT00390000000227; -.
DR HOGENOM; CLU_074702_1_1_1; -.
DR InParanoid; Q8MSW4; -.
DR OMA; DVVYSIH; -.
DR PhylomeDB; Q8MSW4; -.
DR BioGRID-ORCS; 40096; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CG9666; fly.
DR GenomeRNAi; 40096; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036856; Expressed in saliva-secreting gland and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008988; F:rRNA (adenine-N6-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IDA: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 Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..213
FT /note="rRNA N6-adenosine-methyltransferase Mettl5"
FT /id="PRO_0000453466"
FT BINDING 28
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 31
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
FT BINDING 108..109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9NRN9"
SQ SEQUENCE 213 AA; 23978 MW; F31493DEF24463D2 CRC64;
MARLKLRKLE EYLQGVDGFE QPKILLEQYP TPPHIAACMA HHMQSQHEDI EGKLVGDLGC
GCGMLSIAST LLGAQLTVGF ELDGDAVDTF RGNVVEMELP NVDCVRADVL QLIGSKWEKS
FDTVLMNPPF GTKHNAGMDM RFLEVALRLA NRAVYSLHKT STRSYIQKKA LEWGARGSVV
AELRYNIDAS YKFHKQKSKD IEVDFWRFEI GTE
