NSUN5_CAEEL
ID NSUN5_CAEEL Reviewed; 439 AA.
AC Q9NAA7; Q9NAA8; U4PB26;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=26S rRNA (cytosine-C(5))-methyltransferase nsun-5 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:33283887, ECO:0000269|PubMed:33289480, ECO:0000305|PubMed:25635753};
DE AltName: Full=5-methylcytosine rRNA methyltransferase nsun-5;
DE AltName: Full=NOL1/NOP2/Sun domain family member 5 {ECO:0000303|PubMed:25635753};
DE AltName: Full=RNA cytosine C(5)-methyltransferase nsun-5 {ECO:0000305};
DE AltName: Full=rRNA cytosine C(5)-methyltransferase nsun-5 {ECO:0000305};
GN Name=nsun-5 {ECO:0000303|PubMed:25635753, ECO:0000312|WormBase:Y53F4B.4b};
GN ORFNames=Y53F4B.4 {ECO:0000312|WormBase:Y53F4B.4b};
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=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).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30977983; DOI=10.33594/000000067;
RA Adamla F., Rollins J., Newsom M., Snow S., Schosserer M., Heissenberger C.,
RA Horrocks J., Rogers A.N., Ignatova Z.;
RT "A Novel Caenorhabditis Elegans Proteinopathy Model Shows Changes in mRNA
RT Translational Frameshifting During Aging.";
RL Cell. Physiol. Biochem. 52:970-983(2019).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33289480; DOI=10.7554/elife.56205;
RA Heissenberger C., Rollins J.A., Krammer T.L., Nagelreiter F., Stocker I.,
RA Wacheul L., Shpylovyi A., Tav K., Snow S., Grillari J., Rogers A.N.,
RA Lafontaine D.L., Schosserer M.;
RT "The ribosomal RNA m5C methyltransferase NSUN-1 modulates healthspan and
RT oogenesis in Caenorhabditis elegans.";
RL Elife 9:0-0(2020).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=33283887; DOI=10.15252/embj.2020105496;
RA Navarro I.C., Tuorto F., Jordan D., Legrand C., Price J., Braukmann F.,
RA Hendrick A.G., Akay A., Kotter A., Helm M., Lyko F., Miska E.A.;
RT "Translational adaptation to heat stress is mediated by RNA 5-
RT methylcytosine in Caenorhabditis elegans.";
RL EMBO J. 0:0-0(2020).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase which
CC methylates the carbon-5 position of cytosine 2381 to 5-methylcytosine
CC (m5C2381) in 26S rRNA (PubMed:25635753, PubMed:33289480,
CC PubMed:33283887). Plays a role in the production of mature 5S, 5.8S,
CC 18S and 26S rRNAs and promotes the processing of the internally
CC transcribed spacer 2 (ITS2), which separates the 5.8S and 26S rRNAs on
CC large pre-rRNA precursors (PubMed:33289480). May play a role in the
CC translation of leucine and proline codons (Probable). May play a role
CC in maintaining ribosomal frameshifting in response to osmotic stress
CC (PubMed:30977983). Not required for global translation
CC (PubMed:33289480). {ECO:0000269|PubMed:25635753,
CC ECO:0000269|PubMed:30977983, ECO:0000269|PubMed:33283887,
CC ECO:0000269|PubMed:33289480, ECO:0000305|PubMed:33283887}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in 26S rRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in 26S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:66588, Rhea:RHEA-COMP:17065, Rhea:RHEA-COMP:17066,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:33283887, ECO:0000269|PubMed:33289480,
CC ECO:0000305|PubMed:25635753};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:Y53F4B.4b};
CC IsoId=Q9NAA7-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:Y53F4B.4a};
CC IsoId=Q9NAA7-2; Sequence=VSP_060574;
CC Name=c {ECO:0000312|WormBase:Y53F4B.4c};
CC IsoId=Q9NAA7-3; Sequence=VSP_060575;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown increases lifespan and
CC stress resistance (PubMed:25635753). RNAi-mediated knockdown results in
CC a higher frequency of gene products that arise as a consequence of
CC increased ribosomal frameshifting in response to osmotic stress induced
CC by high salt concentrations in adults (PubMed:30977983). RNAi-mediated
CC knockdown does not result in fertility defects (PubMed:33283887).
CC {ECO:0000269|PubMed:25635753, ECO:0000269|PubMed:30977983,
CC ECO:0000269|PubMed:33283887}.
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; BX284602; CAB70100.3; -; Genomic_DNA.
DR EMBL; BX284602; CAB70101.2; -; Genomic_DNA.
DR EMBL; BX284602; CDH93054.1; -; Genomic_DNA.
DR RefSeq; NP_001293548.1; NM_001306619.1. [Q9NAA7-3]
DR RefSeq; NP_497088.3; NM_064687.5.
DR RefSeq; NP_497089.2; NM_064688.4.
DR AlphaFoldDB; Q9NAA7; -.
DR SMR; Q9NAA7; -.
DR IntAct; Q9NAA7; 1.
DR STRING; 6239.Y53F4B.4b; -.
DR EPD; Q9NAA7; -.
DR PaxDb; Q9NAA7; -.
DR PeptideAtlas; Q9NAA7; -.
DR EnsemblMetazoa; Y53F4B.4a.1; Y53F4B.4a.1; WBGene00013151. [Q9NAA7-2]
DR EnsemblMetazoa; Y53F4B.4a.2; Y53F4B.4a.2; WBGene00013151. [Q9NAA7-2]
DR EnsemblMetazoa; Y53F4B.4a.3; Y53F4B.4a.3; WBGene00013151. [Q9NAA7-2]
DR EnsemblMetazoa; Y53F4B.4b.1; Y53F4B.4b.1; WBGene00013151. [Q9NAA7-1]
DR EnsemblMetazoa; Y53F4B.4c.1; Y53F4B.4c.1; WBGene00013151. [Q9NAA7-3]
DR GeneID; 175153; -.
DR UCSC; Y53F4B.4a; c. elegans.
DR CTD; 175153; -.
DR WormBase; Y53F4B.4a; CE39655; WBGene00013151; nsun-5. [Q9NAA7-2]
DR WormBase; Y53F4B.4b; CE35679; WBGene00013151; nsun-5. [Q9NAA7-1]
DR WormBase; Y53F4B.4c; CE49086; WBGene00013151; nsun-5. [Q9NAA7-3]
DR eggNOG; KOG2360; Eukaryota.
DR GeneTree; ENSGT00940000155974; -.
DR HOGENOM; CLU_005316_7_4_1; -.
DR InParanoid; Q9NAA7; -.
DR OMA; IQMGKHP; -.
DR OrthoDB; 987359at2759; -.
DR PhylomeDB; Q9NAA7; -.
DR PRO; PR:Q9NAA7; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00013151; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9NAA7; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:1900035; P:negative regulation of cellular response to heat; IMP:UniProtKB.
DR GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:2000234; P:positive regulation of rRNA processing; IMP:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..439
FT /note="26S rRNA (cytosine-C(5))-methyltransferase nsun-5"
FT /id="PRO_0000449822"
FT ACT_SITE 366
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 313
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT VAR_SEQ 1..154
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060574"
FT VAR_SEQ 1..64
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060575"
SQ SEQUENCE 439 AA; 49839 MW; E5F35F3D05EB3DDC CRC64;
MATDALYNEV AEIIRCVLAK EKSVRNAVYG SSYKNKKALL RLSCESLKFR PVFDEILQDK
ELKSMKRDAN IGGSVELLYV LMYETLVGSG LTRCSQELKS VISRRIQRIK EVEHAMQDEG
RGIKAMKEAD DGMKKIQIPR YARINTLKWT ADEAMKTLET EKWKILGTLK PENFAEMVTK
MKDDEVYVDP HVENLIIFAP NIQNFYEYWM VEQRYLILQD KASCLPAFLL NPRPGSQVFD
TCAAPGMKTS HAAAIMENQG KVWAMDRAAD RVATMKQLLD ASKVAIASSF CGDFLKTDVT
DKKFSKVKFA IVDPPCSGSG IVKRMDEITG GNAEKERLEK LKNLQAMILK HALKLPGLKR
AVYSTCSVHE EENEQVVDEV LLDTYVRQNY VLKKNVLPEW TYRGLKTYEV GEHCLRANPK
VTLTNGFFVA VFERVKSSE
