NSUN5_DROME
ID NSUN5_DROME Reviewed; 433 AA.
AC Q9VDZ4;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=28S rRNA (cytosine-C(5))-methyltransferase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9NAA7};
DE AltName: Full=NOL1/NOP2/Sun domain family member 5 {ECO:0000305};
GN Name=Nsun5 {ECO:0000303|PubMed:25635753, ECO:0000312|FlyBase:FBgn0259704};
GN ORFNames=CG42358 {ECO:0000312|FlyBase:FBgn0259704};
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 DISRUPTION PHENOTYPE.
RX PubMed=25635753; DOI=10.1038/ncomms7158;
RA Schosserer M., Minois N., Angerer T.B., Amring M., Dellago H.,
RA Harreither E., Calle-Perez A., Pircher A., Gerstl M.P., Pfeifenberger S.,
RA Brandl C., Sonntagbauer M., Kriegner A., Linder A., Weinhaeusel A.,
RA Mohr T., Steiger M., Mattanovich D., Rinnerthaler M., Karl T., Sharma S.,
RA Entian K.D., Kos M., Breitenbach M., Wilson I.B., Polacek N.,
RA Grillari-Voglauer R., Breitenbach-Koller L., Grillari J.;
RT "Methylation of ribosomal RNA by NSUN5 is a conserved mechanism modulating
RT organismal lifespan.";
RL Nat. Commun. 6:6158-6158(2015).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the C(5) position of a cytosine in 28S rRNA.
CC {ECO:0000250|UniProtKB:Q9NAA7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in 28S rRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in 28S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47788, Rhea:RHEA-COMP:11915, Rhea:RHEA-COMP:11916,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:Q9NAA7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47789;
CC Evidence={ECO:0000250|UniProtKB:Q9NAA7};
CC -!- DISRUPTION PHENOTYPE: Increased lifespan and stress resistance.
CC {ECO:0000269|PubMed:25635753}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR EMBL; AE014297; AAF55642.1; -; Genomic_DNA.
DR EMBL; AY069449; AAL39594.1; -; mRNA.
DR RefSeq; NP_650787.1; NM_142530.3.
DR AlphaFoldDB; Q9VDZ4; -.
DR SMR; Q9VDZ4; -.
DR IntAct; Q9VDZ4; 2.
DR STRING; 7227.FBpp0289234; -.
DR PaxDb; Q9VDZ4; -.
DR PRIDE; Q9VDZ4; -.
DR DNASU; 7354421; -.
DR EnsemblMetazoa; FBtr0299957; FBpp0289234; FBgn0259704.
DR GeneID; 7354421; -.
DR KEGG; dme:Dmel_CG42358; -.
DR CTD; 55695; -.
DR FlyBase; FBgn0259704; Nsun5.
DR VEuPathDB; VectorBase:FBgn0259704; -.
DR eggNOG; KOG2360; Eukaryota.
DR GeneTree; ENSGT00940000155974; -.
DR HOGENOM; CLU_005316_7_5_1; -.
DR InParanoid; Q9VDZ4; -.
DR OMA; NRGAVDN; -.
DR OrthoDB; 1128973at2759; -.
DR PhylomeDB; Q9VDZ4; -.
DR BioGRID-ORCS; 7354421; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 7354421; -.
DR PRO; PR:Q9VDZ4; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0259704; Expressed in adult abdomen and 44 other tissues.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; RNA-binding; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..433
FT /note="28S rRNA (cytosine-C(5))-methyltransferase"
FT /id="PRO_0000449823"
FT ACT_SITE 357
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 235..241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96P11"
FT BINDING 259
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 286
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 304
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 433 AA; 49280 MW; 535CC484FD66C083 CRC64;
MSKKPHSIKV PTQYRATAKI LKAALEQQKC IKTLIFAEKH ARTRSLHTVL KKFSENRVAL
EKAIEETGLL RDNPSFDPSL AKILVTELLF GRKELNGESK PVQTVRSYKD RLLNSIRDFG
VQRKEPNPRY VRINTNLYSL AEALDYLHKS DWRRKELPAD ASYADFLTAI KSLAENEFMT
DLHVEGVLIF PAKWSNYWVR HPLVHSKRFI LQNKATCLAA ELLAPPSGAT VLDMCAAPGM
KTVHICNVMQ NKGCIYSVEQ DHVRYNTLCE ITKDAGCDIV KPILGDALNL TPERFPDVEY
ILVDPSCSGS GMQNRMTVCD EPKEDKRLQK LQGLQIKILS HAMGAFPNVK RIAYCTCSLW
KEENEQVVQR CLQLNPSFKL LSCKKALRNK WHNVGDKDYP NIGKNVLYCQ PDSDLTDGIF
LALFEKRREG EKD
