NSUN1_CAEEL
ID NSUN1_CAEEL Reviewed; 664 AA.
AC Q9TYV5; A0A0M7RDQ9;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=26S rRNA (cytosine-C(5))-methyltransferase nsun-1 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01023, ECO:0000269|PubMed:33283887, ECO:0000269|PubMed:33289480};
DE AltName: Full=5-methylcytosine rRNA methyltransferase nsun-1 {ECO:0000305};
DE AltName: Full=NOL1/NOP2/Sun domain family member 1 {ECO:0000312|WormBase:W07E6.1a};
DE AltName: Full=RNA cytosine C(5)-methyltransferase nsun-1 {ECO:0000305};
DE AltName: Full=rRNA cytosine C(5)-methyltransferase nsun-1 {ECO:0000305};
GN Name=nsun-1 {ECO:0000312|WormBase:W07E6.1a};
GN Synonyms=nol-1 {ECO:0000312|WormBase:W07E6.1a},
GN nol-2 {ECO:0000312|WormBase:W07E6.1a};
GN ORFNames=W07E6.1 {ECO:0000312|WormBase:W07E6.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
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 [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-439.
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: Methyltransferase which methylates the carbon-5 position of
CC cytosine 2982 to 5-methylcytosine (m5C2982) in 26S rRNA
CC (PubMed:33289480, PubMed:33283887). May play a role in the translation
CC of leucine and proline codons (Probable). May be required for the
CC translation of specific mRNAs such as mRNAs involved in gonad
CC development, collagen production and cuticle integrity
CC (PubMed:33289480). Plays a role in ensuring the correct localization of
CC the germline-specific protein gld-1 during development
CC (PubMed:33289480). Not required for pre-rRNA processing, the production
CC of mature 5S, 5.8S, 18S or 26S rRNAs or global translation
CC (PubMed:33289480). Plays a role in positively regulating fertility
CC (PubMed:33283887). {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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:W07E6.1a};
CC IsoId=Q9TYV5-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:W07E6.1b};
CC IsoId=Q9TYV5-2; Sequence=VSP_061010;
CC -!- DEVELOPMENTAL STAGE: Expression increases during the larval stages to
CC adulthood. {ECO:0000269|PubMed:33289480}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in L1 larvae results in
CC sterility (PubMed:33283887). RNAi-mediated knockdown in adults results
CC in reduced egg-laying (PubMed:33289480). RNAi-mediated knockdown from
CC day 0 of adulthood or in the germline does not affect lifespan
CC (PubMed:33289480). RNAi-mediated knockdown in somatic tissues reduces
CC lifespan by 10% and reduces body length and results in morphological
CC defects in the gonad leading to the production of no oocytes
CC (PubMed:33289480). RNAi-mediated knockdown increases resistance to heat
CC stress and increases the speed of locomotion (PubMed:33289480). RNAi-
CC mediated knockdown disrupts the localization of the germline-specific
CC protein gld-1, results in collagen deposition and increases cuticle
CC permeability (PubMed:33289480). RNAi-mediated knockdown reduces the
CC methylation of cytosine to 5-methylcytosine (m5C) in 26S rRNA
CC (PubMed:33289480). RNAi-mediated knockdown does not affect the
CC methylation of cytosine 2381 to 5-methylcytosine (m5C2381) in 26S rRNA
CC (PubMed:33289480). {ECO:0000269|PubMed:33283887,
CC ECO:0000269|PubMed:33289480}.
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; CCD73642.1; -; Genomic_DNA.
DR EMBL; BX284602; CUR29991.1; -; Genomic_DNA.
DR PIR; D88022; D88022.
DR PIR; T33803; T33803.
DR RefSeq; NP_001303796.1; NM_001316867.1. [Q9TYV5-2]
DR RefSeq; NP_493742.1; NM_061341.5. [Q9TYV5-1]
DR AlphaFoldDB; Q9TYV5; -.
DR SMR; Q9TYV5; -.
DR IntAct; Q9TYV5; 1.
DR STRING; 6239.W07E6.1; -.
DR EPD; Q9TYV5; -.
DR PaxDb; Q9TYV5; -.
DR PeptideAtlas; Q9TYV5; -.
DR EnsemblMetazoa; W07E6.1a.1; W07E6.1a.1; WBGene00021073. [Q9TYV5-1]
DR EnsemblMetazoa; W07E6.1b.1; W07E6.1b.1; WBGene00021073. [Q9TYV5-2]
DR GeneID; 173437; -.
DR KEGG; cel:CELE_W07E6.1; -.
DR UCSC; W07E6.1; c. elegans. [Q9TYV5-1]
DR CTD; 173437; -.
DR WormBase; W07E6.1a; CE28259; WBGene00021073; nsun-1. [Q9TYV5-1]
DR WormBase; W07E6.1b; CE51106; WBGene00021073; nsun-1. [Q9TYV5-2]
DR eggNOG; KOG1122; Eukaryota.
DR GeneTree; ENSGT00940000161554; -.
DR HOGENOM; CLU_005316_3_1_1; -.
DR InParanoid; Q9TYV5; -.
DR OMA; FLAIPHM; -.
DR OrthoDB; 1239772at2759; -.
DR PhylomeDB; Q9TYV5; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00021073; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q9TYV5; 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:0042335; P:cuticle development; IMP:UniProtKB.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:UniProtKB.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
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:1905516; P:positive regulation of fertilization; IMP:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:1901046; P:positive regulation of oviposition; IMP:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
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; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023273; RCMT_NOP2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02012; RCMTNOP2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00446; nop2p; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Nucleus; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..664
FT /note="26S rRNA (cytosine-C(5))-methyltransferase nsun-1"
FT /id="PRO_0000452476"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..81
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..664
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 439
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 313..319
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 337
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 382
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT VAR_SEQ 1..253
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061010"
FT MUTAGEN 439
FT /note="C->A: In mj437; viable and produce viable progeny.
FT Reduces body length. Increases the reduction in body
FT length, and at 25 degrees Celsius there is a reduced number
FT of progeny in a nsun-4 (mj457), nsun-2 (mj458) and nsun-5
FT (tm3898) mutant background. Abolishes methylation of
FT carbon-5 cysteines and its metabolic derivative 2'-O-
FT methyl-5-hydroxymethylcytosine in RNA in a nsun-4 (mj457),
FT nsun-2 (mj458) and nsun-5 (tm3898) mutant background."
FT /evidence="ECO:0000269|PubMed:33283887"
SQ SEQUENCE 664 AA; 73905 MW; B5D2B1C00C4DFE09 CRC64;
MAIVKKKKVS AASKAATEKP EVKKAVKRPV AETEAVTPKK KKLVKKVKKS AKKAHEEEPI
EQVEKLQLID DDEDGLEGLS FPGSDDEDLR DDYSDDDSDA GDHLPIEKKS AALDKQKEKI
IAEGEEELQL NIANQATFEL PTVEEIENEM KSVPNLEIVK QRIADVIQVL GDFKNRRDPQ
KSRENYVEVL KKDLCSQYGY NDYLMGKFMD LFPNGAELLE FLEANDNPRP VTIRANSLKV
KRRDLAKNLI NRGMNVDPAA DWTKVGLVVY DSQVPVGATP EYLAGHYMIQ GLNSLLPVMA
LAPQPGDRVL DMCSAPGGKT SHIAALMKNS GVLFANDANF TRCRAIIGNL HRLGVNNTVV
CNLGGEEFSK IRPNGFDRIL LDAPCSGTGV IWKDQSVKTS KDSQDVQRRH TMQRQLILSA
LDSLDANSPN GGYLVYSTCS VLVEENEAVV NFLLERRHCE LVPTGLSIGV DGYTRFRDYR
FHPSLSMTKR YYPHVHNIDG FYVAKIKKLS NAKMSKQGVM EKEKEKAAQK SQNKKNKAEA
EASESSDDEE EKKNGVEVNG QKKPAKKQQQ KKQKADGDDS DDDNNAPMKN IGSGARANKK
RRNQKKAAEK QAAVKEDDGF NTVGNVKRAK KPTQFKSKVP KRAAARTGAK SVKNRRKKML
AKQQ
