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Database: UniProt
Entry: A0A0D9RJG5_CHLSB
LinkDB: A0A0D9RJG5_CHLSB
Original site: A0A0D9RJG5_CHLSB 
ID   A0A0D9RJG5_CHLSB        Unreviewed;       469 AA.
AC   A0A0D9RJG5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=NOP2/Sun RNA methyltransferase 6 {ECO:0000313|Ensembl:ENSCSAP00000008754.1};
GN   Name=NSUN6 {ECO:0000313|Ensembl:ENSCSAP00000008754.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000008754.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000008754.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000008754.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; AQIB01160576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01160577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008000624.1; XM_008002433.1.
DR   AlphaFoldDB; A0A0D9RJG5; -.
DR   SMR; A0A0D9RJG5; -.
DR   STRING; 60711.ENSCSAP00000008754; -.
DR   Ensembl; ENSCSAT00000010665.1; ENSCSAP00000008754.1; ENSCSAG00000012571.1.
DR   GeneID; 103237969; -.
DR   KEGG; csab:103237969; -.
DR   CTD; 221078; -.
DR   eggNOG; KOG1122; Eukaryota.
DR   GeneTree; ENSGT00940000155370; -.
DR   OMA; YQGAMLY; -.
DR   OrthoDB; 1077100at2759; -.
DR   BioGRID-ORCS; 103237969; 0 hits in 9 CRISPR screens.
DR   Proteomes; UP000029965; Chromosome 9.
DR   Bgee; ENSCSAG00000012571; Expressed in pituitary gland and 7 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:Ensembl.
DR   GO; GO:0000049; F:tRNA binding; IEA:Ensembl.
DR   GO; GO:0002946; P:tRNA C5-cytosine methylation; IEA:Ensembl.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd21150; PUA_NSun6-like; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF34; TRNA (CYTOSINE(72)-C(5))-METHYLTRANSFERASE NSUN6; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS50890; PUA; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          141..466
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        373
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         242..248
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         266
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         293
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         323
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   469 AA;  51794 MW;  1235B3143E4E75AF CRC64;
     MSIFPKISLR PEVENYLKEG FVNKEIVTAL GKQEAERKFE TLLKHLSHPP SFTTVRVNTH
     LASVQHVKNL LLDELQKQFN GLSIPILQHP DLQDVLLIPV IGPRKNIKKQ QCEAIVGAQC
     GNAVLRGAHV YAPGIVSASK FMKAGDVVSV YSDIKGKCKK GAREFDGTKV FLGNGISELS
     RKEIFSGLPE LKGMGIRMTE PVYLSPSFDN VLPRYLFLQN LPSALVTHVL NPQPGEKILD
     LCAAPGGKTT HIAALMHDQG EVIALDKIFS KVEKIKQNAL LLGLNSIRAF CFDGTKAVKL
     DMVEDTEGEP PFLPESFDRI LLDAPCSGMG QRPNMACTWS LKELASYQPL QRKLFTAAVQ
     LLKPEGVLVY STCTITLAEN EEQVAWALTK FPCLQLQPQE PQIGGEGMRG AGLSCEQLKQ
     LQRFDPSAVP LPDTDMDSLR EARREDMLRL ANKDSIGFFV AKFVKCKST
//
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