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Database: UniProt
Entry: A0A2I3GGT8_NOMLE
LinkDB: A0A2I3GGT8_NOMLE
Original site: A0A2I3GGT8_NOMLE 
ID   A0A2I3GGT8_NOMLE        Unreviewed;       340 AA.
AC   A0A2I3GGT8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=NOP2/Sun RNA methyltransferase 3 {ECO:0000313|Ensembl:ENSNLEP00000030507.1};
GN   Name=NSUN3 {ECO:0000313|Ensembl:ENSNLEP00000030507.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000030507.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000030507.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000030507.1}
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|PROSITE-ProRule:PRU01023}.
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DR   EMBL; ADFV01005477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003261743.1; XM_003261695.3.
DR   AlphaFoldDB; A0A2I3GGT8; -.
DR   SMR; A0A2I3GGT8; -.
DR   STRING; 61853.ENSNLEP00000030507; -.
DR   Ensembl; ENSNLET00000054891.1; ENSNLEP00000030507.1; ENSNLEG00000028997.1.
DR   GeneID; 100602825; -.
DR   KEGG; nle:100602825; -.
DR   CTD; 63899; -.
DR   GeneTree; ENSGT00940000153665; -.
DR   InParanoid; A0A2I3GGT8; -.
DR   OMA; FNRFNYP; -.
DR   OrthoDB; 317522at2759; -.
DR   Proteomes; UP000001073; Chromosome 21.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:Ensembl.
DR   GO; GO:0070129; P:regulation of mitochondrial translation; IEA:Ensembl.
DR   GO; GO:0002127; P:tRNA wobble base cytosine methylation; IEA:Ensembl.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 6.20.240.40; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22808:SF8; TRNA (CYTOSINE(34)-C(5))-METHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:UP000001073};
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          44..334
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         139..145
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         193
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         211
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   340 AA;  38434 MW;  8D16D1659B6974FE CRC64;
     MLTRLKAKSE GKLAKQICKV VLDHFEKQYS KELGDAWNTV REILTSPSCW QYAVLLNRFN
     YPFELEKDLH LKGYHTLFQG SLPNYPKSMK CYLSRTPGRI PSERHQIGNL KKYYLLNAAS
     LLPVLALELR DGEKVLDLCA APGGKSIALL QCACPGYLHC NEYDSLRLRW LRQTLESFIP
     QPLINVINVS ELDGRKMGDA QPEMFDKVLV DAPCSNDRSW LFSSDSQKAS RRISQRRNLP
     LLQIELLRSA IKALRPGGIL VYSTCTLSKA ENQDVISEIL NSHSNIMPMD IKGIARTCSH
     DFTFAPTGQE CGLLVIPDKG KAWGPMYVAK LKKSWSTGKW
//
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